THE SEVERE ACUTE RESPIRATORY SYNDROME CORONA VIRUS All documents cited herein are incorporated by reference in their entirety. RELATED APPLICATIONS, FROM WHICH PRIORITY IS CLAIMED This application incorporates by reference in its entirety US provisional patent application 60/462,218, Attorney Reference No. PP20474.001, filed on April 10, 2003 via Express Mail with the US post office, US provisional patent application 60/462,465, Attorney Reference No. PP20480.001, filed on April 11, 2003 via Express Mail with the US post office, US provisional patent application 60/462,418, Attorney Reference No. PP20480.002, filed on April 12, 2003 via Express Mail with the US post office, US provisional patent application 60/462,748, Attorney Reference No. PP20480.003, filed on April 13, 2003 via Express Mail with the US post office, US provisional patent application 60/463,109, Attorney Reference No. PP20480.004, filed on April 14, 2003 via Express Mail with the US post office, US provisional patent application 60/463,460, Attorney Reference No. PP20480.005, filed on April 15, 2003 via Express Mail with the US post office, US provisional patent application 60/463,668, Attorney Reference No. PP20480.006, filed on April 16, 2003 via Express Mail with the US post office, US provisional patent application 60/463,983, Attorney Reference No. PP20480.007, filed on April 17, 2003 via Express Mail with the US post office, US provisional patent application 60/463,971, Attorney Reference No. PP20480.008, filed on April 18, 2003 via Express Mail with the US post office, US provisional patent application 60/464,899, Attorney Reference No. PP20480.009, filed on April 22, 2003 via Express Mail with the US post office, US provisional patent application 60/464,838, Attorney Reference No. PP20507.001, filed on April 22, 2003 via Express Mail with the US post office, US provisional patent application 60/465,273, Attorney Reference No. PP20518.001, filed on April 23, 2003 via Express Mail with the US post office, US provisional patent application 60/465,535, Attorney Reference No. PP20518.002, filed on April 24, 2003 via Express Mail with the US post office, US provisional patent application 60/468,312, Attorney Reference No. PP20480.010, filed on May 5, 2003 via Express Mail with the US post office, and US provisional patent application 60/473,144, Attorney Reference No. PP20480.011, filed on May 22, 2003, US provisional patent application 60/495,024, Attorney Reference No. PP20480.012, filed on August 14, 2003 via Express Mail with the US post office, US provisional patent application 60/505,652, Attorney Reference No. PP20480.013, filed on September 23, 2003 via Express Mail with the US post office, US provisional patent application 60/510,781, Attorney Reference No. PP20480.014, filed on October 11, 2003 via Express Mail with the US post office, US provisional patent application 60/529,464, Attorney Reference No. PP20480.015, filed on December 11, 2003 via Express Mail with the US post office, US provisional patent application 60/536,177, Attorney Reference No. PP20480.016, filed on January 12, 2004 via Express Mail with the US post office, and US provisional patent application 60/ , , Attorney Reference No. PP20480.017, filed on April 7, 2004 via Express Mail with the US post office. FIELD OF THE INVENTION The invention relates to nucleic acids and proteins from Severe Acute Respiratory Syndrome (SARS) Virus. These nucleic acids and proteins can be used in the preparation and manufacture of vaccine formulations for the treatment or prevention of SARS. The invention also relates to diagnostic reagents, kits (comprising such reagents) and methods which can be used to diagnose or identify the presence or absence of a SARS virus in a biological sample. The invention also relates to methods for the treatment or prevention of SARS utilizing small molecule viral inhibitors and combinations of small molecule viral inhibitors and kits for the treament of SARS . BACKGROUND OF THE INVENTION An outbreak of a virulent respiratory virus, now known as Severe Acute Respiratory Syndrome (SARS), was identified in Hong Kong, China and a number of other countries around the world in 2003. Patients typically had symptoms including fever, dry cough, dyspnea, headache, and hypoxemia. Isolates of the SARS virus appear to have homology with at least the RNA polymerase gene of several known coronaviruses. A phylogenetic analysis of this homology is presented in Peiris et al, "Coronavirus as a possible cause of severe acute respiratory syndrome", Lancet, published online April 8, 2003 at http://image.ihelancet.com/extras/03art3477web.pdf, incorporated herein by reference in its entirety. Other sequenced fragments of the SARS virus genome appear to overlap with the open reading frame lb of coronaviruses. See, Drosten et al, "Identification of a Novel Coronavirus in Patients with Severe Acute Respiratory Syndrome", New England Journal of Medicine, published online at http://www.nejm.org on April 10, 2003, incorporated herein by reference in its entirety. The Genome Science Center in British Colombia, Canada published on its website (http://www.bcgsc.ca/bioinfo/SARS/) a draft genome assembly of 29,736 base pairs of a virus believed to be a SARS virus, referred to as the TOR2 isolate. This draft genome assembly is given herein as SEQ ID NO: 1. The Centers for Disease Control (CDC) published a nucleotide sequence of a SARS-CoV strain (SEQ ID NO: 2) on its website (http://www.cdc.gov/ncidod/sars/pdf/nucleoseq.pdf). The CDC has also published a phylogenetic tree of the predicted N, S and M proteins (attached as FIGURE 6). This tree places the SARS virus outside any of the previously known coronavirus groups. There is a growing need for prophylactic or therapeutic vaccines against the SARS virus as well as diagnostic and screening methods and compositions to identify the presence of the virus in, e.g., mammalian tissue or serum. SUMMARY OF THE INVENTION The invention relates to nucleic acids and proteins from Severe Acute Respiratory Syndrome (SARS) virus. These nucleic acids and proteins can be used in the preparation and manufacture of vaccine formulations for the treatment or prevention of SARS. Such vaccine formulations may include an inactivated (or killed) SARS virus, an attenuated SARS virus, a split SARS virus preparation and a recombinant or purified subunit formulation of one or more SARS viral antigens. Expression and delivery of the polynucleotides of the invention may be facilitated via viral vectors and/or viral particles. The invention also relates to diagnostic reagents, kits (comprising such reagents) and methods which can be used to diagnose or identify the presence or absence of a SARS virus in a biological sample. The invention further includes non-coding SARS viral polynucleotide sequences, SARS viral sequences encoding for non-immunogenic proteins, conserved and variant SARS viral polynucleotide sequences for use in such diagnostic compositions and methods. The invention further relates to vaccine formulations comprising one or more SARS virus antigens and one or more other respiratory virus antigens. Additional respiratory virus antigens suitable for use in the invention include antigens from influenza virus, human rhinovirus (HRN), parainfluenza virus (PIN), respiratory syncytial virus (RSN), adenovirus, metapneumovirus, and rhinovirus. The additional respiratory virus antigen could also be from a coronavirus other than the SARS coronavirus. Preferably, the additional respiratory virus antigen is an influenza viral antigen. The compositions of the invention may further comprise one or more adjuvants. Adjuvants suitable for use in the invention include mucosal, fransdermal or parenteral adjuvants. Mucosal adjuvants suitable for use in the invention include detoxified bacterial ADP-ribosylating toxins, such as E. coli heat labile toxoids (e.g., LTK63), chitosan and derivatives thereof, and non-toxic double mutant forms of Bordetella pertussis toxoids. Parenteral adjuvants suitable for use in the invention include MF59 and aluminum or aluminum salts. The invention also provides methods for treating SARS by administering small molecule compounds, as well as methods of identifying potent small molecules for the treatment of SARS. In one aspect of the invention a method of identifying a therapeutically active agent is provided comprising: (a) contacting the therapeutically active agent with a cell infected with the SARS virus; (b) measuring attenuation of a SARS related enzyme. In a more particular embodiment, the therapeutically active agent is a small molecule. In another more particular embodiment, the therapeutically active agent is a nucleoside analog. In another more particular embodiment the therapeutically active agent is a peptoid, oligopeptide, or polypeptide. In another embodiment the SARS related enzyme is SARS protease. In another embodiment the SARS related enzyme is SARS polymerase. In still another embodiment the SARS related enzyme is a kinase. Methods of identifying therapeutically active agents for treatment of SARS virus infection are further discussed in Section N below. In another aspect of the invention a method of treating a human infected with SARS is provided comprising administering a small molecule to a patient in need thereof. In one embodiment the small molecule is an inhibitor of SARS protease. In another embodiment the small molecule is an inhibitor of SARS polymerase. In another embodiment the SARS related enzyme is a kinase. In still another embodiment the small molecule is administered orally or parenterally. The invention also provides the use of such small molecules in the manufacture of a medicament for the treatment of severe acute respiratory syndrome. Small molecule compounds of the present invention include those of less than 1000 g/mol, preferably with an aromatic region and greater than one heteroatom selected from O, S, or Ν. Preferred small molecules include, but are not limited to acyclovir, gancyclovir, vidarabidine, foscamet, cidofovir, amantidine, ribavirin, trifluorothymidine, zidovudine, didanosine, zalcitabine, and combinations thereof. Interferons may also be used for treating patients, including interferon-α and interferon-β. Interferon treatment has shown promise in treating SARS in monkeys (Enserink (2004) Science 303: 1273-1275), particularly when pegylated (Haagmans et al. (2004) Nature Medicine 10:290-293). One aspect of the present invention relates to methods for identifying individuals exposed to, and biological samples containing SARS virus (SARSN), and to kits for carrying out the methods. Such methods can utilize nucleic acid detection techniques such as PCR, RT-PCR (the Coronaviridae are RΝA viruses), transcription-mediated amplification (TMA), ligase chain reaction (LCR), branched DΝA signal amplification assays, isothermal nucleic acid sequence based amplification (ΝASBA), other self-sustained sequence replication assays, boomerang DΝA amplification, strand-displacement activation, cycling probe technology, or combinations of such amplification methods. Such nucleic acid detection techniques utilize oligonucleotides having nucleotide sequence similar to, or complementary to, the SARS viral genome, as primers (e.g., for amplification) and as probes (e.g., for capture or detection), as is well known in the art. Alternatively, or in addition to the nucleic acid detection methods described supra, the methods of the present invention can utilize various immunoassay techniques for detection of SARSN antigens and/or antibodies. Accordingly, the present invention relates to methods of identifying individuals exposed to SARSN, or biological samples containing SARSN, by detecting the presence of SARSN antigens using antibodies which specifically bind to the same. The antibodies are preferably monoclonal antibodies. Quantification of the amount of viral antigens present in a sample of an individual may be used in determining the prognosis of an infected individual. Preferably, the SARSN antigens to be detected are generally one of the structural proteins, particularly those present on the surface of the viral particles and include, for example, the spike glycoprotein (S), also called E2; the envelope (small membrane) protein (E), also called sM; the membrane glycoprotein (M), also called El; the hemagglutinin-esterase glycoprotein (HE); also called E3; and the nucleocapsid phosphoprotein (Ν). In preferred embodiments, the antigens to be detected are the S, E and M proteins using antibodies to the same. The present invention relates to kits for identifying individual SARSN and reagents used in such kits. The kits comprise a first container which contains antibodies which specifically bind to a SARSN antigen and a second container which contains the SARSN antigen. The antibodies are preferably monoclonal antibodies. The kits may be adapted for quantifying the amount of antigen in a sample of an individual. Such information may be used in determining the prognosis of an infected individual. The present invention relates to methods of identifying individuals exposed to SARS virus, or biological samples containing SARSN, by detecting the presence of antibodies against SARS virus antigen in a sample using SARS antigen. Quantification of the amount of anti-S ARS protein from SARS antibodies present in a sample of an individual may be used in determining the prognosis of an infected individual. Any one or more of the viral proteins (structural proteins or nonstructural proteins) may be used as antigen to detect the SARSN antibodies; preferably a SARSN antigen that is conserved amoung SARSN isolates is preferred. In this regard, nonstructural protein (e.g., Pol, Hel, 3CLp, MP, PLP1, PLP2) may be particularly useful. The present invention relates to kits for identifying individuals exposed to SARS and reagents used therein. The kits comprise a first container which contains antibodies which were produced in response to exposure to an antigen from SARS virus and a second container which contains the SARS antigen(s). The kits may be adapted for quantifying the amount of anti-SARS antibodies present in a sample of an individual. Such information may be used in determining the prognosis of an infected individual. The present invention relates to methods of identifying individuals exposed to SARS virus, or biological samples containing SARSN, by detecting the presence of nucleic acid from SARS virus. Quantification of the amount of SARS nucleic acid present in a sample of an individual may be used in determining the prognosis of an infected individual. The methods utilize oligonucleotide probes and/or primers that are similar or complementary in sequence to the SARSN genome or transcription or replication products. Preferred probes and primers are described herein. Also included in the present invention are kits for carrying out the methods of detecting the SARSN nucleic acid. The invention further includes a method for the treatment and/or prevention of SARS through the administration of a therapeutically effective amount of at least one antiviral compound from among those described in the US Patents and published international patent applications listed in Table 1 and Table 2. In one embodiment of the method, the antiviral compound is a small molecule. In another embodiment, the antiviral compound is a protease inhibitor. In a further embodiment, the antiviral protease inhibitor is a 3C-like protease inhibitor and/or a papain-like protease inhibitor. In another embodiment, the antiviral compound is an inhibitor of an RΝA-dependent RΝA polymerase. hi another embodiment, a first antiviral compound which is a protease inhibitor is administered with a second antiviral compound which is an RΝA-dependent RΝA polymerase inhibitor. The invention further provides for the administration of a steroidal anti-inflammatory drug in combination with at least one antiviral compound, for example, from the antiviral compounds described in the documents listed in Table l and Table 2. The invention further provides for a method for the treatment and/or prevention of SARS through the administration of a therapeutically effective amount of at least one antiviral compound from among those described in the US Patents and published international patent applications listed in Table 1 and Table 2 by inhalation. In one embodiment of the method, the antiviral compound is a small molecule. In another embodiment, the antiviral compound is a protease inhibitor. In a further embodiment, the antiviral protease inhibitor is a 3C-like protease inhibitor and/or a papain-like protease inhibitor. In another embodiment, the antiviral compound is an inhibitor of an RΝA dependent RΝA polymerase. In another embodiment, a first antiviral compound which is a protease inhibitor is administered with a second antiviral compound which is an RΝA-dependent RΝA polymerase inhibitor. The invention further provides for the administration of a steroidal anti-inflammatory drug in combination with at least one antiviral compound, for example, from the antiviral compounds described in the documents listed in Table 1 and Table 2 by inhalation. The steroidal anti-inflammatory drug may be administered by inhalation for a local effect or administered for systemic absorption such as via an oral or intravenous route. The invention further provides the use of an antiviral compound, as defined above, in the manufacture of a medicament for the treatment of severe acute respiratory syndrome. The invention further provides for a kit for use by a consumer for the treatment and/or prevention of SARS. Such a kit comprises: (a) a pharmaceutical composition comprising a therapeutically effective amount of at least one antiviral compound from among those described in the US Patents and published international patent applications listed in Table 1 and Table 2 and a pharmaceutically acceptable carrier, vehicle or diluent; (b) a container for holding the pharmaceutical composition; and, optionally; (c) instructions describing a method of using the pharmaceutical compositions for the treatment and or the prevention of SARS. The kit may optionally contain a plurality of antiviral compounds for the treatment of SARS wherein the anti viral compounds are selected from 3C-like protease inhibitors and papain-like protease inhibitors. In a further embodiment, the kit contains an antiviral compound which is an RNA- dependent RNA polymerase inhibitor. When the kit comprises more than one antiviral compound, the antiviral compounds contained in the kit may be optionally combined in the same pharmaceutical composition. An additional aspect of the invention provides for the use of at least one of the antiviral compounds described in the US Patents and published international patent applications listed in Table 1 and Table 2 for the manufacture of a medicament for the treatment or prevention of SARS. BRIEF DESCRIPTION OF THE DRAWINGS FIGURE 1: Schematic of coronavirus genome organization. FIGURE 2: Schematic of coronavirus ORFla/ORFlb gene products. FIGURE 3 (A - C): Alignment of coronavirus polynucleotide sequences for selected genes (including nucleocapsid (N), matrix (M), and hemagluttinin-esterase (HE)). FIGURE 4 (A - F): Alignment of coronavirus polypeptide sequences (including ORFla/ORFlb, nucleocapsid (NP), hemagluttinin-esterase (HE), envelope (Sm or E), matrix (M), and spike (S). FIGURE 5: Alignment of spike (S) polypeptide sequences, taken from Figure 4, in the region of the junction of the SI and the S2 domains, and protease cleavage site for selected coronaviruses. FIGURE 6: CDC phylogenetic tree of SARS-CoV strain (Clustalx 1.82, neighbor-joining tree). Figure 6A shows coronavirus N protein analysis, Figure 6B shows coronavirus S protein analysis, and Figure 6C shows coronavirus M protein analysis. FIGURE 7: Conserved and specific sequence of the SARS virus. Figures 7A-7D show multiple sequence alignments (CLUSTAL W 1.82) of the structural proteins of the SARS virus genome (7A: PEP4 Spike protein; 7B: PEP7 small membrane protein; 7C: PEP8 matrix glycoprotein; 7D: PEP 13 nucleocapsid protein), which have counterparts in all or some of the other known coronaviruses. Figures 7E-7H show dendrograms reporting the protein distances among the sequences in alignments 7A-7D. Labels 229E: human coronavirus; MEN: murine hepatitis virus; TGN: transmissible gastroenteritis virus; AIBN: avian infectious bronchitis virus; BONLΝE: Bovine coronavirus; PEDN: porcine epidemic diarrhea virus. FIGURE 8: Alignment of the 5'UTR of several coronaviruses, to show consensus nucleotide sequence at the 5'UTR. FIGURE 9: Sequences of preferred primers for amplification of the 5'UTR. F and R denote forward and reverse PCR primers, and the numbers indicate nucleotide positions withing Figure 8. FIGURE 10: Alignment of the 3'UTR of several coronaviruses, to show consensus nucleotide sequence at the 3'UTR. FIGURE 11 : Sequences of preferred primers for amplification of the 3'UTR. F and R denote forward and reverse PCR primers, and numbers indicate nucleotide positions within Figure 10. FIGURE 12: Coiled-coil prediction for SEQ ID NO: 6042, using Coils program (Figure 12A) or LearrCoil (Figure 12B). FIGURE 13: Example of insertion of a reporter gene-of -interest at a site between exisiting SARS virus genes. Small nonstructural gene products are not depicted schematically. FIGURE 14: Schematic depicting representative examples of SARS virus replicons. Small nonstructural gene products are not depicted schematically. FIGURE 15: SARS virus nsp2 proteinase (3CLp) and identification of catalytic and substrate sites. FIGURE 16: alignment of SARS virus nsp2 proteinase (3CLp) with that of avian LBV, MHV, and BCoN. Residues in dotted boxes are key residues the substrate sites (F, Y & H); residues in solid boxes are catalytic cysteine (C) and histidine (H) residues. FIGURE 17: Genome organization of SARS coronavirus. Replicase and structural regions are shown, along with the predicted products of cleavage within ORFla and ORFlb. The position of the 5' RΝA leader sequence (L), the 3' poly(A) tract and the ribosomal frame-shift consensus between ORFla and ORFlb are also indicated. Each box represent a protein product. They are shaded according to the level of amino acid identity with corresponding proteins of other coronaviruses (see also Table 2). The SARS-specific genes are white. Positions of the 9 SARS- specific six-base IG sequences (5'-ACGAAC-3'; SEQ LD NO 7293) are indicated by arrows. FIGURE 18: Genome organization of Coronaviruses representative of group 1 (HCoN-229E, accession number: AF304460), group 2 (mouse hepatitis virus MHV, accession number: ΝC_001846), group 3 (avian infectious bronchitis virus ALBN, accession number: ΝC_001451) and SARS coronavirus. Other completely sequenced coronaviruses used in this study are available at the following accession numbers: porcine epidemic diarrhea virus (PEDN), AF353511; transmissible gastroenteritis virus (TGN), ΝC_002306; Bovine coronavirus (BCoN): AF220295. Red boxes represent group-specific genes. The position of the leader RΝA sequence 5 and poly(A) tract is also indicated in genomes where they are reported. The position of specific IG sequences is indicated by circles of different shades. In the SARS genome^ we also find three IG sequences specific for group 2 coronavirus. . FIGURE 19: Topological model predicted for the spike protein anchored to the viral membrane. Structural and predicted functional domains are indicated. The Ν-terminal region (SI) is .0 predicted to contain the receptor binding domain. Two coiled coil regions within the S2 domain, partially superimposed to leucine zipper motifs are presumably involved in oligomerization. The hydrophobic domain is responsible for membrane anchoring. FIGURE 20: Phylogenetic tree obtained from the multiple sequence alignment of a 922 bp internal region of the. pol gene from 12 coronaviruses and SARS. Numbers at the nodes represent L5 the result of a bootstrap analysis and strongly support the branches. Sequences not available within the complete coronavirus genomes have been retrieved from GenBank at the following accession numbers: hemagglutinating encephalomyelitis virus of swine (PHEV), AF124988, Human OC43 virus (OC43), AF124989, canine coronavirus (CCV), AF124986, feline infectious peritonitis virus (FJPN), AF124987, turkey coronavirus (TCN), AF124991, syaloacryoadenitis 20 virus of rats (SDAN), AF124990. FIGURE 21: 21A. Unrooted tree obtained from the alignment of consensus sequences of the group I and group II SI domain of spike proteins (Gl_cons and G2_cons) with those of a group 3 spike (ALBN) and the spike of SARS virus. The number indicates the result of a bootstrap analysis. The sequences used to generate the consensus profile from group 1 are: HcoN-229E, 5 accession number P15423; porcine epidemic diarrhea virus (PEDN), ace no: ΝP_598310; transmissible gastroenteritis virus (TGV), ace no: NP_058424; Canine coronavirus (CCV), ace no: S41453; porcine respiratory virus (PRV), ace no: S24284; feline infectious peritonitis virus (FTPV), ace no: VGIH79. The sequences used to generate the consensus profile from group 2 are: mouse hepatitis virus (MHV), ace no: NP_045300; Bovine coronavirus (BCoV), ace no: 0 NP_150077; Human coronavirus OC43, ace no: P36334; hemagglutinating encephalomyelitis virus of swine (PHEV), ace no: AAL80031; for group 3, only the sequence of the spike protein of avian infectious bronchitis virus (AIBV), ace no: AAO34396 was used. 21B: Schematic representation of cysteine positions in SI domains of group 1, 2 and 3, compared to the SARS spike. Horizontal bars represent the SI amino acid sequences (in the case of SARS and AIBV) or 5 the consensus profiles (generated from group 1, Gl_cons, and from group 2, G2_cons). The length of the bars are not to scale. Relative cysteine positions are indicated by rectangle bars. Only cysteines perfectly conserved within each consensus are reported. Lines connect cysteines conserved between the SARS SI domain and the consensus sequences as shown. FIGURE 22: illustration of a Neisseria Adhesin A protein (NadA). FIGURE 23: Raw translation from SARS coronavirus genome (reading frame +1). FIGURE 24: Raw translation from SARS coronavirus genome (reading frame +3) FIGURE 25: lb and Spike open reading frames, separated by *. FIGURE 26: SARS growth in vero cells. FIGURE 27: chromatogram of the capture step of SARS coronavirus on Matrix Cellufine Sulfate Superformance 150/10. Analysis was on 100ml coronoavirus harvest. The left Y axis shows absorbance at 280nm. The right Y axis shows the gradient (%B). The X axis shows the volume (ml). FIGURE 28: Silver-stained MCS chromatography fractions. Lanes are: (1) marker; (2) coronavirus vero cell harvest; (3) coronavirus vero cell harvest, after 0.65μm filtration; (4) flowthrough; (5) wash; (6) 20% peak (virus peak). Lanes were loaded with 1 μg of test protein. FIGURE 29: Western Blot of MCS chromatography fractions. Lanes are as described for Fig.28. FIGURE 30: Linear density gradient ultracentrifugation, 15-60% sucrose (SW28, 2 hours, 20000 rpm). The graph shows protein concentration (■) and sucrose concentration (♦). FIGURE 31: Silver-stained density gradient fractions on NuPage 4-12% Bis-Tris-Ge (Novex), reduced conditions, heated for 10 minutes at 70°C. Lanes are: (1) marker; (2) 20% peak MCS; (3) density gradient fraction 11; (4) density gradient fraction 12; (5) density gradient fraction 13; (6) density gradient fraction 14; (7) density gradient fraction 15; (8) density gradient fraction 16; (9) density gradient fraction 17. The bulk of proteins was in fractions 15 to 17. Lanes 2, 8 and 9 were loaded with lμg protein. FIGURE 32: Chromatogram of the Capture Step of SARS coronavirus on MCS. Details are as for Figure 27, except that 200ml harvest was used. FIGURE 33: Silverstain (left) and Western Blot (right) of chromatographic fractions. Lanes are as described for Figures 28 and 29, except that lane (6) is the 5% peak. Treatment before SDS-PAGE was at room temperature for 30 minutes. FIGURE 34: Density Gradient Ultracentrifugation, 15-40% sucrose (SW28, 2 hours, 20000 rpm). The graph shows protein concentration (■) and sucrose concentration (♦). FIGURE 35: Silverstain (left) and Western Blot (right) of Density Gradient Ultracentrifugation fractions on NuPage 4-12% Bis-Tris-Ge (Novex), reduced conditions. Lanes are: (1) marker; (2) density gradient fraction 6; (3) density gradient fraction 7; (4) density gradient fraction 8; (5) density gradient fraction 9; (6) density gradient fraction 10; (7) density gradient fraction 15. Fractions 7-10 (lanes 3-6) contained pure coronavirus proteins. The bulk of impurities was in fraction 15 (lane 7). Lanes 2, 8 and 9 were loaded with ~lμg protein. Treatment before SDS-PAGE was at room temperature for 30 minutes. FIGURE 36: EM pictures of Density Gradient Fractions 8-10. Figure 36A shows fraction 8; Figure 36B shows fraction 9; Figure 36C shows fraction 10. FIGURE 37: Spike/Nad A fusion constructs. FIGURES 38 and 39: Results of the expression in E.coli of S1 L , SlL-NadA and SlL-NadA Λ an chor - Figure 38 shows SDS-PAGE analysis of total lysates from BL21(DE3)/pET, BL21(DE3)/pET- SIL and BL21(DE3)/pET-Sl -NadAΛanchor- The bands are indicated by an arrow, and the three lanes are, from left to right: BL21(DE3)/pET; BL21(DE3)/pET-Sl L ; BL21(DE3)/pET- S l L -NadA Δanc hor. Figure 39 shows (39A) SDS-PAGE and (39B) western blot analyses of total lysates from BL21(DE3)/pET, BL21(DE3)/pET-Sl L -NadA (grown under un-induced condition) and BL21(DE3)/pET-SlL-NadA (grown under induced condition). The bands are indicated by an arrow, and lanes are, from left to right: BL21(DE3)/pET; BL21(DE3)/pET-Sl L -NadA; BL21(DE3)/pET-Sl L -NadA. The western blot shows the presence of oligomeric forms of the protein. FIGURE 40: Schematic of SARS Spike clones. FIGURE 41: Transient Expression of SARS Spike Proteins (western blot of COS7 cell lysate). Each lane of the 4-20% TG SDS gel was loaded with 20μg cell lysate (total 1.2mg). The labeling antibodies are shown. FIGURE 42: Western blot analyses of COS7 cell lysates on 4% TG SDS gel showing oligomerization state of intracellular S molecules. FIGURE 43: Western blot analyses of COS7 cell lysates on 4-20% TG SDS gel showing Transient Expression of SARS Spike Proteins. Lanes are: (1) mock, AF; (2) mock, DF; (3) nSh, AF; (4) nSh, DF; (5) nShΔTC, AF; (6) nShΔTC, DF. Each lane was loaded with 5μl of each sample, 400μl total. The blot was labeled with antibody against the His-tagged protein. FIGURE 44: Western blot analyses of COS7 cell medium on 4-20% TG SDS gel showing Transient Expression of SARS Spike Proteins. Truncated spike protein is secreted. Spike proteins were purified from the culture medium (from a 10cm plate), first by a ConA column and then finally by His « tag Magnetic beads. Each lane was loaded with one third of the material. FIGURE 45: Western blot analyses of COS7 cell lysates on 4-20% TG SDS gel showing glycoslation of SARS spike proteins. In the two left-hand blots (lanes 1-5), samples were boiled in SDS and β-mercaptoethanol; in the two right-hand blots (lanes 6-11), samples were in SDS only, with no boiling. Lanes 1-8 were labeled with a monoclonal raised against the His-tag protein; labes 9-11 were labeled with rabbit anti-S ARS antibody. FIGURE 46: Effect of SARS spike protein expression on cell viability. FIGURE 47: Western blot analyses of COS7 cell lysates on 4% TG SDS gels showing oligomerization state of intracellular spike molecules. Blots were labeled with anti-His-tag mAb. The membrane fraction of COS7 cell lysate was fractionated by a sizing column before loading the lanes. Fractions 7 to 14 show bands with kDa values of: 71000, 1400, 898, 572, 365,232, 148 and 99, respectively. FIGURE 48: Fractionation of cells into aqueous and detergent fractions. FIGURE 49: Schematic of constructs for use in OMV preparation. FIGURE 50: SARS HR1 and HR2 constructs. FIGURE 51: Vaccine protection froms SARS in Balb/c mouse model. FIGURE 52: Expressed on Spike protein in transfected 293 cell lysates (52A) or COS7 cell culture supematants (52B). Proteins were separated on 4-20% TG SDS gels. The label was anti- His-tag, except for the right-hand three lanes of 52B, where the label was rabbit anti-S ARS serum. In Figure 52A, the left-hand three lanes were treated with DTT and were boiled, but neither treatment was used for the right-hand three lanes. In Figure 52B, no DTT was used, but all lanes were heated to 80°C for 5 minutes. FIGURE 53: Western blot of Spike proteins expressed in COS7 cells. Proteins were incubated at room temperature (RT), 80°C or 100°C to check for any effect on molecular weight. FIGURE 54 shows similar experiments on SARS virions. FIGURE 55: Results of a pulse chase experiment, showing expression and processing of SARS spike protein following infection with alphavirus replicon particles. Cells were freated with or without EndoH as shown. FIGURE 56: Effect of heating on Spike protein trimers. FIGURE 57: Coomassie blue-stained gel of yeast-expressed proteins. Lanes are: 1-See Blue Standard (lOjul); 2-pAB24 gbl (20μg); 3-S ARS Spike S 1 c.1 gbl (20 g); 4-SARS Spike S 1 c.2 gbl (20μg); 5-See Blue Standard (lOμl); 6-pAB24 ip (5μl); 7-SARS Spike SI c.l (5μl); 8-SARS Spike SI c.2 (5μl). FIGURES 58 to 64: Schematics of preparation of yeast expression constructs. FIGURES 65 to 66: Yeast-expressed sequences for Spike. FIGURE 67: Western blots showing expression of SARS spike protein from alphavirus replicon particles and replicon RNA. Figure 67A was run under non-reducing conditions and at room temperature (i.e. no heating), with lanes: (1) VEE/SL -spike infection; (2) VEE/SL -GFP infection; (3) Replicon-spike RNA transfection; (4) Replicon-GFP RNA transfection. Figure 67B was run with SARS virions at different temperatures, as shown. FIGURE 68: induction of antibody responses in mice. Vaccine groups are: (1) Inactivated SARS Virus; (2) Truncated Recombinant Spike Protein; (3) Full length Spike: DNA+DNA.PLG+ Alphavirus; (4) Full length Spike: Alphavirus particles only. FIGURE 69: Binding of human monoclonal antibody S3.2 to purified truncated Spike protein. The X-axis shows antibody concentration, and the Y-axis shows ELISA absorbance. The interpolation result is 2158.13. FIGURE 70: Geometric mean ELISA titers of antibodies induced by the SARS-CoV spike protein delivered as different vaccines (left to right: inactivated virus; 3/xg truncated spike protein; 75/ g DNA encoding truncated spike protein. FIGURE 71: Neutralization titers after immunization with (left) nSdΔTC protein or (right) DNA encoding nSdΔTC, delivered on PLG. FIGURE 72: Correlation between the spike antigen binding and neutralizing antibodies FIGURE 73: Western blot of CHO cell lines expressing Spike protein in full-length form (left) or in truncated form (right). Proteins were separated by 4-12% SDS-PAGE, with boiling in DTT and staining by polyclonal serum. FIGURE 74: Structural components of SARS-CoV spike glycoprotein and expression construct. L denotes leader peptide (residues 1-13), TM the transmembrane, and Cy the cytoplasmic tail segments. The hexa-His tags are not shown. FIGURE 75: Western blot analysis of SARS spike proteins expressed in COS7 cells. In Figure 75A, COS7 cells were transfected with indicated plasmid constructs and the expressed proteins in cell lysates 48 hr post-fransfection were analysed by SDS-PAGE (4-20% polyacrylamide) in reducing and denaturing condtions, with proteins visualized by anti-histidine Mab. In Figure 75B, proteins were collected from cell culture medium 48 hr post-transfection and purified first by a ConA column and then by His-tag magnetic beads. Purifed proteins were analysed by SDS- PAGE (4-20% polyacrylamide) and were visualized by anti-S ARS rabbit serum. FIGURE 76: Endo H sensitivity of C-terminal truncated spike protein (SΔ) found in cell lysate (lanes 1,2) and culture medium (lanes 3,4). Positions of internal SΔ protein and secreted SΔ protein are marked with arrow heads. FIGURE 77: Oligomeric status of the SARS spike protein. Recombinant S protein oligomer in COS7 cells transfected with the full-length spike construct (nSh). The cell lysates were treated with DTT and/or heat as indicated above each lane. The different forms of S protein in treated and untreated samples were visualized by SDS-PAGE (4% polyacrylamide) and Western blot analysis using anti-histidine MAb. FIGURE 78: Effect of heat denaturation on the oligomeric status of recombinant S protein in the absence of DTT. The COS7 cell lysates were heated before the electrophoresis as indicated and the S proteins were visualized as described fogiFigure 77. FIGURE 79: Effect of heat denaturation on the oligomeric status of spike protein in SARS virion particles. SARS-CoV were grown in Vero cells, purified and solubilized from the virion particles by SDS, heat-denatured as indicated and visualized as described in Figure 77, except that rabbit antiserum against the purified virus was used as a probe. FIGURE 80: Analysis of the oligomeric status of SARS virion spike protein by cross-linking experiment. Solubilized SARS virion proteins were treated with DMS. Both untreated (-) and DMS treated (+) virion proteins were heat denatured in the absence of DTT and visualized by 4% PAGE followed by silver staining. FIGURES 81 & 82: Analysis of the oligomeric status of truncated spike protein by heat denaturation. Truncated spike protein within COS7 cell lysates (81) or secreted into culture medium (82) were heat denatured as indicated in the absence of DTT and visualized by Western blot analysis. FIGURE 83: Reactivity of deglycosylated full-length spike oligomer with conformational and non-conformational antibody. The full-length recombinant spike oligomer was partially deglycosylated with PNGase F in non denaturating condition and visualized by Western blot analysis using anti-histidine Mab (lane 1,2,3) or rabbit antiserum against purified SARS CoV (lane 4,5,6). FIGURE 84: Localization of expressed SARS spike proteins in fractionated COS7 cell lysate visualized by western blot. Cells were transfected with indicated plasmids and lysed with Dounce homogeniser in hypotonic buffer 48 hr post transfection. Cell lysate was centrifuged to obtain soluble cytosol and insoluble membrane fraction that was further solublized by 4% Triton X-100. Proteins were heated with SDS at 80 C and analysed by SDS-PAGE (4-20% polyacrylamide) in reducing condtion. Proteins were visualized by anti-histidine Mab. The cytosol fractions were loaded in lanes 1, 3, and 5 and the membrane fractions were loaded in lanes 2, 4, and 6. FIGURE 85: Intracellular and surface expression of recombinant full-length (A,D) or truncated (B,E) spike protein in COS7 cells. The cells were fixed at 48 hrs posttransfection and either treated with detergent (Cytofix/perm, BD Biosciences) for intracellular immunofluorescence (A,B,C) or with 2% paraformaldehyde for cell surface immunofluorescence observation (D,E,F) at x40 magnification. Mock transfected cells (C,F) were included as controls. FIGURES 86-105: SDS-PAGE od E.coli expressed proteins. Tot = total protein; Sol = soluble protein fraction. Labels are protein names (Tables 26-30). FIGURE 106: Immunofluorescence after administration of vector encoding optimsed N antigen. FIGURE 107: Lnmunofluorescence of (A) native and (B) codon-optimsed M sequences. FIGURE 108: Immunofluorescence of (A) native and (B) codon optimsed E sequences. FIGURES 109-111: Western blots of Vero cells using rabbit antibodies obtained after immunization with spike proteins expressed in E.coli. FIGURE 112: Spike protein expression in 293 cells. Lanes: (M) Markers; (1) Mock transfected; (2,6) cells expressing nS protein, lysate; (3,7) cells expressing nSdTC protein, lysate; (4,8) cells expressing nS protein, supernatant; (5,9) (4) cells expressing nSdTC protein, supernatant. Staining antibody: (2 to 5) mouse serum obtained after DNA immunization; (6 to 9) rabbit serum obtained after immunization with whole killed virus. FIGURE 113: Six reading frames of SEQ ID NO: 9968. FIGURE 114: Six reading frames of SEQ LD NO: 10033. FIGURE 115: Alignment of bovine coronavirus pol lab (top row; SEQ ID NO: 10068), avian infectious bronchitis pol lab (second row; SEQ ID NO: 10069), murine hepatitis virus pol lab (third row; SEQ ID NO: 10070), SEQ ID NO s : 9997/9998 (fourth row) and a consensus sequence (bottom row; SEQ ID NO: 10071). FIGURE 116: Schematic of coronavirus genome organization. FIGURE 117: Schematic of coronavirus ORFla/ORFlb gene products, including "*" region. FIGURE 118: Alignment. FIGURE 119: Alternative start codons within SEQ ID NO: 10080. FIGURE 120: Six reading frames of SEQ ID NO: 10084. FIGURE 121: Alignment of SEQ ID NO: 10033 and SEQ ID NO: 10084. FIGURE 122: Reading frames in SEQ ID NO: 10084. FIGURE 123: Start codon analysis for SEQ ID NO: 10084. FIGURE 124: BLAST analysis of SEQ ID NO: 10210. FIGURE 125: Epitope analysis of SEQ JD NO: 10210 by either (13A) Hopp & Woods or (13B) Kyte & Doolittle. FIGURE 126: Reading frames in SEQ ID NO: 10299. FIGURE 127: Reading frames in SEQ ID NO: 10505. FIGURE 128: Reading frames in SEQ ID NO: 11563. FIGURE 129: Reading frames in SEQ ID NO: 10033. FIGURE 130: Alignment of SEQ JX> NO: 9997 and SEQ JD NO: 10033. FIGURE 131: Reading frames in SEQ ID NO: 10299. FIGURE 132: Reading frames in SEQ ID NO: 10505. FIGURE 133: Western Blot of SARS protease purification fractions. FIGURE 134: Cleavage of DABCYL-EDANS (a fluorescent tagged peptide with a SARS protease cleavage site) by SARS protease at different concentrations. The graph shows activity/concentration correlations with no protease (♦), 0.95 uM protease (■) and 2.86 uM protease (•). In the event of a discrepancy between a sequence in the sequence listing and a sequence in the drawings, the drawings should take precedence. DETAILED DESCRIPTION OF THE INVENTION The practice of the present invention will employ, unless otherwise indicated, conventional methods of chemistry, biochemistry, molecular biology, immunology and pharmacology, within the skill of the art. Such techniques are explained fully in the literature. See, e.g., Remington's Pharmaceutical Sciences, Mack Publishing Company, Easton, Pa., 19th Edition (1995); Methods In Enzymology (S. Colowick and N. Kaplan, eds., Academic Press, Inc.); and Handbook of Experimental Immunology, Vols. I-IV (D.M. Weir and CC. Blackwell, eds., 1986, Blackwell Scientific Publications); Sambrook, et al, Molecular Cloning: A Laboratory Manual (2nd Edition, 1989); Handbook of Surface and Colloidal Chemistry (Birdi, K.S. ed., CRC Press, 1997); Short Protocols in Molecular Biology, 4th ed. (Ausubel et al. eds., 1999, John Wiley & Sons); Molecular Biology Techniques: An Intensive Laboratory Course, (Ream et al, eds., 1998, Academic Press); PCR (Introduction to Biotechniques Series), 2nd ed. (Newton & Graham eds., 1997, Springer Verlag); Peters and Dalrymple, Fields Virology (2d ed), Fields et al. (eds.), B.N. Raven Press, New York, NY. All publications, patents and patent applications cited herein, are hereby incorporated by reference in their entireties. Severe Acute Respiratory Syndrome (SARS) virus has recently been identified as a new viral species. The SARS viral species includes the following isolates. - two virus isolates described in Peiris et al. "Coronavirus as a possible cause of severe acute respiratory syndrome" Lancet published online at http://image.thelancet.com/extras/03art3477web.pdfon April 8 2003, incorporated herein by reference in its entirety and the sequences deposited with GenBank at accession number AY268070. - the isolates and viral sequences described in Drosten et al. , "Identification of a Novel Coronavirus in Patients with Severe Acute Respiratory Syndrome", New England Journal of Medicine, published online at http://www.nejm.org on April 10, 2003. - the isolates and viral sequences described on the website of the WHO network on March 25 and 24, 2003. - the isolates and viral sequences described in Tsang et al. , "A Cluster of Cases of Severe Acute Respiratory Syndrome in Hong Kong" New England Journal of Medicine, published online at http://www.nejm.org on March 31, 2003. - the isolates and viral sequences described in Poutanen et al. , "Identification of Severe Acute Respiratory Syndrome in Canada" New England Journal of Medicine, published online at http://www.nejm.org on March 31 , 2003. As described in the Lancet article, a 646 base pair polynucleotide from the SARS virus has weak homology to viruses of the family Cornoaviridae. The Lancet article further reports that a deduced amino acid sequence (of 215 amino acids) from this sequence has about 57% sequence homology to the RNA polymerase of bovine coronavirus and murine hepatitis virus. Phylogenetic analysis of the protein sequences are also presented in the Lancet article showing that the polymerase sequence is most closely related to the group II coronaviruses. Additional SARS viral isolates can be identified, isolated and/or sequenced by virologists skilled in the art. Virologists can readily identify new viral isolates as a SARS virus. Criteria which a virologist may use to identify new SARS isolates include: sequence homology of the new isolate to known SARS viral isolates; similar genomic organization of the new viral isolate to known SARS viral isolates; immunological (serologic) similarity or identity with known SARS viral isolates; pathology; and similarity of virion morphology with known SARS viral isolates; and similarity of infected cell morphology as that caused by known SARS viral isolates (visualized, for instance, by electron microscopy). Methods for isolating and sequencing SARS viral isolates include the methods described by Peiris et al. in the Lancet paper. As reported in the Lancet paper, RNA from clinical samples can be reverse transcribed with random hexamers and cDNA can be amplified with primers having sequences of SEQ JD NOS: 6584 & 6585 in the presence of 2.5 mmol/L magnesium chloride (94°C for 1 min, 50°C for 1 min, and 72°C for 1 min). Reverse transcription of a viral isolate using random hexamers can be accomplished in an RT-PCR assay as follows. Virus isolates are propagated on mammalian cells, particularly fetal rhesus kidney cells. Total RNA from virus-infected and virus-uninfected fetal rhesus kidney cells is then isolated. RNA samples are reverse transcribed with a primer having SEQ JD NO: 6586. cDNA can be amplified by a primer having SEQ JD NO: 6587. Unique PCR products (in size) in the infected cell preparation are then cloned and sequenced, and genetic homology of the sequence compared with those in GenBank. One skilled in the art would be able to identify and clone additional genomic regions using a variety of standard cloning techniques, such as, for example, using random primer RT-PCR and detection of sequences overlapping one or more of the above sequences, and/or using oligonucleotide primers, e.g., degenerate primers, based on the sequences provided herein (see Figures 1-5, Figures 8-11, SEQ JD NOS: 3-20). Cloning, sequencing and identification of SARS virus by one skilled in the art can be further facilitated by the use of polynucleotide sequences, particularly RNA polymerase sequences, from related Coronaviruses. Sequence homology of new viral isolates with the known SARS isolates described above can be readily determined by one skilled in the art. New SARS isolates may be identified by a percent homology of viral nucleotide sequences of 99%, 95%, 92%, 90%, 85%, or 80% homology of the new virus to known SARS viral polynucleotide sequences. New SARS isolates may also be identified by percent homology of 99%, 95%, 92%, 90%, 85%, or 80% homology of the polypeptides encoded by the polynucleotides of the new virus and the polypeptides encoded by known SARS virus. New SARS isolates may also be identified by a percent homology of 99%, 95%, 92%, 90%, 85%, or 80% homology of the polynucleotide sequence for specific genomic regions for the new virus with the polynucleotide sequence for specific genomic regions of the known SARS viruses. Additionally, new SARS isolates may be identified by a percent homology of 99%, 95%, 92%, 90%, 85%, or 80% homology of the polypeptide sequence encoded by the polynucleotide of specific genomic regions of the new SARS virus to the polypeptide sequence encoded by the polynucleotides of specific regions of the known SARS virus. These genomic regions may include regions (e.g., gene products) which are typically in common among numerous coronaviruses, as well as group specific regions (e.g., antigenic groups), such as, for example, any one of the following genomic regions which could be readily identified by a virologist skilled in the art: 5'untranslated region (UTR), leader sequence, ORFla, ORFlb, nonstructural protein 2 (NS2), hemagglutinin-esterase glycoprotein (HE) (also referred to as E3), spike glycoprotein (S) (also referred to as E2), ORF3a, ORF3b, ORF3x, nonstructural protein 4 (NS4), envelope (small membrane) protein (E) (also referred to as sM), membrane glycoprotein (M) (also referred to as El), ORF5a, ORF5b, nucleocapsid phosphoprotein (N), ORF7a, ORF7b, intergenic sequences, 3'UTR, or RNA dependent RNA polymerase (pol). The SARS virus may have identifiable genomic regions with one or more the above-identified genomic regions. A SARS viral antigen includes a protein encoded by any one of these genomic regions. A SARS viral antigen may be a protein or a fragment thereof, which is highly conserved with coronaviruses. A SARS viral antigen may be a protein or fragment thereof, which is specific to the SARS virus (as compared to known comaviruses). (See, Figures 1-5, Figures 8-11, SEQ JD NOS: 3-20). One skilled in the art could also recognize electron microscopy of a SARS virus infected mammalian cell. Electron microscopy of SARS infected cells are shown in the Lancet paper. As discussed in the paper, electron microscopy of negative stained (3% potassium phospho- tungstate, pH 7.0) ultracentrifuged cell-culture extracts of SARS infected fetal rhesus Mdney cells show the presence of pleomorphic enveloped virus particles of around 80-90 nm (range 70- 130 nm) in diameter with surface morphology compatible with a coronavirus (see Lancet paper, Figure 1). Thin-section electron microscopy of infected cells reveals virus particles of 55-90 nm diameter within smooth walled vesicles in the cytoplasm (see Lancet paper, Figure 2B). Electron microscopy can also be used to observe virus particles at the cell surface. Electron microscopy of a human lung biopsy sample depicts similar viral morphology. See Lancet paper Figure 2A. /. SARS POLYPEPTIDES AND POLYNUCLEOTIDES The invention relates to nucleic acids and proteins from SARS virus. Such polynucleotides and polypeptides are exemplified further below. In one embodiment, the polynucleotides of the invention do not include one of the following five primers, disclosed at http://content.nejm.org/cgi/reprint/NEIMoa030781v2.pdf. SEQ JD NOS: 6034-38. The invention also includes polynucleotide sequences which can be used as probes for diagnostic reagents, kits (comprising such reagents) and methods which can be used to diagnose or identify the presence or absence of a SARS virus in a biological sample. The invention includes a polynucleotide sequence comprising one or more of the primer sequences identified in SEQ JD NOS: 21-1020. The invention further includes polynucleotide sequence comprising the complement of one or more of the primer sequences identified in SEQ JD NOS: 21-1020. The invention includes a polypeptide sequence comprising an amino acid sequence from the sequence shown in Figure 23. Such amino acid sequences are SEQ ID NOS: 6588-6809. The invention includes polypeptides comprising an amino acid sequence having sequence identity to these sequences, and the invention includes a fragment of a polypeptide comprising one of these sequences. The invention includes a polypeptide comprising an amino acid sequence from the sequence shown in Figure 24. Such amino acid sequences are SEQ ID NOS: 6810-7179. The invention includes a protein comprising an amino acid sequence having sequence identity to these sequences, and the invention includes a fragment of a protein comprising one of these sequences. The invention includes a protein comprising SEQ JD NO: 6039. The invention includes a polypeptide comprising an amino acid sequence having sequence identity to SEQ JD NO: 6039. The invention includes a fragment of a polypeptide comprising SEQ JD NO: 6039. The invention includes a diagnostic kit comprising a polypeptide comprising SEQ ID NO: 6039, or a fragment thereof. The invention includes a diagnostic kit comprising a polynucleotide sequence encoding SEQ JD NO: 6039, or a fragment thereof. The invention includes an immunogenic composition comprising a polypeptide comprising SEQ JD NO: 6039, or a fragment thereof. The invention includes an antibody which recognizes a polypeptide comprising SEQ ID NO: 6039, or a fragment thereof. SEQ ID NO: 6039 demonstrates functional homology with ORFla of coronaviruses. Predicted transmembrane or hydrophobic regions of SEQ JD NO: 6039 are identified below. Although the polyprotein of coronaviruses is proteolytically cleaved into numerous smaller proteins, hydrophobic domains in the polyprotein are known to mediate the membrane association of the replication complex and to be able to dramatically alter the architecture of host cell membranes. Accordingly, the hydrophobic domains of the polyprotein are targets for genetic mutation to develop attenuated SARS virus vaccines. The hydrophobic domains are also targets for small molecule inhibitors of the SARS virus. The hydrophobic domains may also be used to generate antibodies specific to those regions to treat or prevent SARS virus infection. Predicted Transmembrane Helices in SEQ XD NO : 6039 The sequence positions in brackets denominate the core region. Only scores above 500 are considered significant. Inside to outside helices 43 found Outside to inside helices : 43 found from to score center from to lore center 100 ( 100) 118 ( 116) 103 107 94 ( 97) 118 ( 112) 291 104 473 ( 473) 488 ( 488) 1003 481 400 ( 400) 418 ( 415) 243 407 529 ( 532) 549 ( 549) 541 539 473 ( 473) 488 ( 488) .113 481 584 ( 584) 606 ( 601) 1049 594 523 ( 528) 548 ( 548) 285 538 773 ( 773) 791 ( 789) 514 782 583 ( 583) 606 ( 601) 662 593 1071 1071)1089 (1086) 243 1078 776 791) 1435 783 1121 1121)1137 (1137) 459 1130 1068 1086) 370 1078 1679 1679)1696 (1696) 404 1686 1121 1137) 455 1130 2098 2102)2119 (2116) 509 2109 1679 1694) 340 1686 2145 2145)2160 (2160) 797 2153 2098 2116) 678 2109 2206 2209)2224 (2224) 2686 2216 2148 2163) 434 2155 2316 2316)2332 (2332) 2123 2325 2208 2226) 2389 2219 2335 2339)2358 (2354) 2101 2346 2309 2326) 1773 2318 2373 2373)2390 (2390) 532 2380 2342 2360) 1666 2353 2597 2600)2615 (2615) 307 2607 2373 2390) 254 2380 2753 2753)2770 (2768) 2242 2760 2753 2770) 2119 2763 2831 2833)2854 (2851) 759 2841 2832 2851) 687 2844 2879 2882)2900 (2897) 526 2889 2858 2873) 253 2866 2990 2996)3012 (3010) 1289 3003 2879 2899) 400 2889 3024 3024)3042 (3039) 2281 3032 2990 3005) 875 2998 3054 3058)3075 (3072) 2536 3065 3020 3042) 2795 3032 3105 3109)3127 (3123) 2010 3116 3059 3075) 2137 3067 3143 3143)3163 (3159) 184 3152 3105 3123) 1902 3115 3253 3255)3272 (3272) 319 3262 3142 3162) 540 3152 3346 3346)3366 (3366) 203 3356 3343 3366) 496 3358 3375 3375)3392 (3392) 305 3384 3437 3453) 848 3444 3438 3438)3455 (3453) 1021 3445 3489 3505) 302 3498 3559 3567)3584 (3581) 1885 3574 3560 3577) 1460 3569 3589 3589)3606 (3604) 2018 3596 3591 3606) 2193 3598 3611 3611)3629 (3629) 2304 3621 3610 3627) 1484 3620 3659 3659)3674 (3674) 1561 3667 3656 3675) 1240 3668 3756 '3758)3777 (3774) 2352 3767 3681 3699) 590 3691 3890 3890)3904 (3904) 485 3897 3710 3728) 1696 3721 3916 3919)3934 (3934) 241 3926 3723 3738) 1670 3730 4035 4035)4051 (4051) 335 4044 3760 3775) 2367 3767 4217 4217)4232 (4232) 272 4224 3881 3900) 249 3892 4239 4239)4257 (4254) 402 4247 4099 4114) 389 4106 4234 4249) 325 4241 4338 4360) 505 4348 Accordingly, the invention includes a polypeptide comprising a fragment of SEQ JD NO: 6039, wherein said fragment comprises an amino acid sequence including one or more of the hydrophobic transmembrane sequences identified above. The invention includes a polypeptide comprising a fragment of SEQ ID NO: 6039 wherein said fragment comprises one or more of the following polypeptide sequences of SEQ ID NO: 6039: 473-488, 529-549, 584-606, 773-791, 2098-2119, 2145-2160, 2206-2224, 2316-2332, 2335-2358, 2373-2390, 2753-2770, 2831-2854, 2879-2900, 2990-3012, 3024-3042, 3054-3075, 3105-3127, 3438-3455, 3559-3584, 3589-3606, 3611-3629, 3659-3674, 3756-3777, 473-488, 583-606, 776-791, 2098-2119, 2208-2231, 2309- 2332, 2342-2368, 2753-2770, 2832-2854, 2990-3005, 3020-3042, 3059-3075, 3105-3127, 3142- 3162, 3437-3453, 3560-3577, 3591-3606, 3610-3627, 3656-3678, 3710-3738, 3723-3738, and 3760-3777. Preferably, the fragment comprises one or more of the following polypeptide sequences of SEQ ID NO: 6039: 2206-2224, 2316-2332, 2335-2358, 2753-2770, 3024-3042, 3054-3075, 3105-3127, 3589-3606, 3611-3629, 3756-3777, 2208-2231, 2753-2770, 3020-3042, 3059-3075, and 3591-3606. Preferably, the fragment comprises one or more of the following polypeptide sequences of SEQ JD NO: 6039: 2206-2224 and 3020-3042. The invention also includes polynucleotides encoding each of the polypeptide fragments identified above. The invention includes an attenuated SARS virus wherein said attenuated SARS virus contains an addition, deletion or substitution in the polynucleotides encoding for one of the hydrophobic domains identified above. The invention also includes a method for creating an attenuated SARS virus comprising mutating a SARS virus by adding, deleting or substituting the viral genome of the SARS virus to alter the coding of one or more of the hydrophobic domains of SEQ ID NO: 6039 identified above. The invention includes an antibody which specifically identifies one or more of the hydrophobic regions of SEQ JD NO: 6039 identified above. The invention includes a small molecule which binds to, interferes with the hydrophobicity of or otherwise disrupts one or more of the hydrophobic regions of SEQ ID NO: 6039 identified above. Predicted N-glycosylation sites of SEQ ID NO: 6039 are identified in the chart below. Prediction of N-glycosylation sites in SEQ ID NO: 6039 Position Potential Jury NGlyc agreement result 48 NGTC SEQ ID NO: 7180 0.6371 (7/9) + 389 NHSN SEQ ID NO: 7181 0.6132 (6/9) + 916 NFSS SEQ ID NO: 7182 0.5807 (7/9) + 1628 NHTK SEQ ID NO: 7183 0.5610 (7/9) + 1696 NKTV SEQ ID NO: 7184 0.5297 (5/9) + 2031 NPTI SEQ ID NO: 9764 0.5299 (5/9) + WARMING : PRO XI. 2249 NSSN SEQ ID NO: 7185 0.6329 (9/9) ++ 2459 NPTD SEQ ID NO: 9765 0.5599 (6/9) + WARNING: PRO XI. 2685 NVSL SEQ ID NO: 7186 0.6071 (8/9) + 4233 NATE SEQ ID NO: 7187 0.6144 (7/9) + Accordingly, the invention comprises a fragment of SEQ JD NO: 6039 wherein said fragment comprises an amino acid sequence which includes one or more of the N-glycosylation sites identified above. Preferably, the fragment comprises one or more sequences selected from the group consisting of SEQ ID NOS: 7180-7187 & 9764-9765. Preferably, the fragment comprises the amino acid sequence NSSN (SEQ ID NO: 7185). The invention includes a polypeptide comprising a fragment of SEQ JD NO: 6039 wherein said fragment does not include one or more of the glycosylation sites identified above. The invention also includes a polynucleotide encoding such a polypeptide. T-epitopes for SEQ ID NO: 6039 are identified in Table 13. The invention includes a polypeptide for use as an antigen, wherein the polypeptide comprises: (a) an amino acid sequence selected from the group consisting of the T-epitope sequences identified as SEQ ID NOS: 7400-7639; (b) an amino acid sequence having sequence identity to an amino acid sequence of (a). The invention further comprising a polynucleotide sequence encoding the polypeptides of (a) or (b). The invention further comprising a method of expression or delivery of such polynucleotides through viral vectors and/or viral particles. The invention further comprises a polypeptide comprising two or more of the T-epitope sequences identified as SEQ ID NOS: 7400-7639, or a polynucleotide encoding such a polypeptide. The use as an antigen is preferably a use: (1) as a T-cell antigen; (2) for generating a complex between a class I MHC protein (e.g. a class I HLA) and a fragment of said antigen; (3) as an antigen for raising a cell-mediated immune response; and/or (4) as an antigen for raising a CTL response. The use preferably protects or treats disease and/or infection caused by a SARS virus. The invention provides the use of a polypeptide in the manufacture of a medicament for immunising a mammal (typically a human) against SARS viral infection wherein the polypeptide is as defined above. The invention provides a method of raising an immune response in a mammal (typically a human), comprising the step of administering to the mammal a polypeptide as defined above, wherein said immune response is a cell-mediated immune response and, preferably, a CTL response. The immune response is preferably protective or therapeutic. The ORFla and ORFlb sequences of coronaviruses are typically translated as a single ORFlab polyprotein. Slippage of the ribosome during translation generates an a-1 frameshift. One region of such slippage is illustrated below: gggttttacacttagaaacacagtctgtaccgtctgcggaatgtggaaaggttatggctgtagttgtga +1 G F T L R N T V C T V C G M W K G Y G C S C D +3 G F Y T - K H S L Y R R N V E R W - - ccaactccgcgaacccttgatgcagtctgcggatgcatcaacgtttttaaacgggtttgcggtgtaagt +1 Q L R E P L M Q S A D A S T F N G F A V - V +3 P T P R T D A V C G C I N V F K R V C G V S gcagcccgtcttacaccgtgcggcacaggcactagtactg (SEQ ID NO: 7224) + 1 Q P V H R A A Q A L V L (SEQ ID NOS: 7225-7226) +3 A A R L T P C G T G T S T (SEQ ID NOS: 7227-7229) which would generate the following translational slippage (SEQ ID NOS: 7230-7231): ccaactccgcgaacccttgatgcagtctgcggatgcatcaacgtttttaaacgggtttgcggtgtaagt Q L R E P L M Q S A D A S T F L N R V C G V S Accordingly, the invention includes a polypeptide comprising SEQ JD NO: 7232. The invention includes a polypeptide comprising an amino acid sequence having sequence identity to SEQ JD NO: 7232. The invention includes a fragment of a polypeptide comprising SEQ ID NO: 7232 The invention includes a diagnostic kit comprising a polypeptide comprising SEQ ID NO: 7232 or a fragment thereof. The invention includes a diagnostic kit comprising a polynucleotide sequence encoding SEQ JD NO: 7232 or a fragment thereof. The invention includes an immunogenic composition comprising a polypeptide comprising SEQ ID NO: 7232 or a fragment thereof. The invention includes an antibody which recognizes a polypeptide comprising SEQ ID NO: 7232 or a fragment thereof. The invention also includes a polypeptide comprising amino acid sequence Xi-X 2 -X 3 , where Xi is SEQ ID NO: 7233, X 2 is from one to ten amino acids, and X 3 is SEQ ID NO: 7234. X 2 can comprise any sequence of one to ten amino acids (SEQ JD NOS: 7235-7244) but, in preferred embodiments, X 2 is selected from the group consisting of F, FL, FLN, FLNR (SEQ JD NO: 7245), FLNRV (SEQ JD NO: 7246) and FLNRVC (SEQ JD NO: 7247). Preferably, X 2 is SEQ JD NO: 7247. These preferred embodiments are shown as SEQ ID NOS: 7248-7253. The invention includes a polypeptide comprising an amino acid sequence having sequence identity to said amino acid sequences Xi-X 2 -X 3 . The invention includes a fragment of a polypeptide comprising said amino acid sequences X 1 -X 2 -X 3 . The invention includes a diagnostic kit comprising a polypeptide comprising said amino acid sequences X ! -X 2 -X 3 or a fragment thereof. The invention includes a diagnostic kit comprising a polynucleotide sequence encoding said amino acid sequences Xi-X 2 -X or a fragment thereof. The invention includes an immunogenic composition comprising a polypeptide comprising said amino acid sequences Xi-X 2 -X 3 or a fragment thereof. The invention includes an antibody which recognizes a polypeptide comprising said amino acid sequences X Ϊ -X 2 -X 3 or a fragment thereof. The amino acid sequences X X 2 -X 3 (i.e. SEQ JD NOS: 7235-7244) demonstrate functional homology with the polyprotein of murine hepatitis virus. This polyprotein is cleaved to produce multiple proteins. Proteins which can be generated from the Xi-X Xs polyprotein, where X 2 is six amino acids (SEQ JD NO: 7240) are listed below. The invention includes a fragment of the amino acid sequence X ! -X 2 -X 3 (i.e. SEQ ID NOS: 7235-7244) wherein the fragment comprises one of the polypeptide sequences identified in the above table. The invention further includes a fragment of the amino acid sequence XrX 2 -X 3 wherein said fragment comprises a polypeptide sequence which has a serine at its N-terminus and a glutamine at its C-terminus. The invention further includes a fragment of the amino acid sequence Xi-X^Xs wherein said fragment comprises a polypeptide sequence which has an Alanine at its N-terminus and a glutamine at its C-terminus. The invention further includes a fragment of the amino acid sequence Xi-X 2 -X 3 wherein said fragment comprises a polypeptide sequence which has a Asparagine at its N-terminus and a glutamine at its C-terminus. The invention further includes a fragment of the amino acid sequence X ! -X 2 -X 3 wherein said fragment comprises a Cysteine at its N-terminus and a Glutamine at its C-terminus. Each of the fragments identified above can be used in fusion proteins. The invention includes a diagnostic kit comprising a polypeptide comprising at least one of the fragments of the amino acid sequence Xi-X 2 -X 3 (i.e. SEQ ID NOS: 7235-7244) identified in the above paragraph. The invention includes a diagnostic kit comprising a polynucleotide sequence encoding at least one of the fragments of the amino acid sequence XrX 2 -X 3 identified in the above paragraph. The invention includes an immunogenic composition comprising a polypeptide comprising at least one of the fragments of the amino acid sequence X ! -X 2 -X 3 identified in the above paragraph. The invention includes an antibody which recognizes a polypeptide comprising at least one of the fragments of the amino acid sequence X ! -X 2 -X 3 identified in the above paragraph. Predicted N-glycosylation sites of the amino acid sequence X ! -X 2 -X when X 2 is six amino acids are identified at the asparagines located at the following amino acid positions 48; 389; 556; 916; 1628; 1696; 1899; 2079; 2249; 2252; 2507; 2685; 3303; 3373; 3382; 3720; 4150; 4233; 4240; 5016; 5280; 5403; 5558; 5650; 5905; 6031; 6130; 6474; 6918; 6973. Accordingly, the invention comprises a fragment of SEQ ID NO: 7239 wherein said fragment is at least ten amino acids and wherein said fragment comprises one or more of the asparagines from the amino acid positions of SEQ JD NO: 7239 selected from the group consisting of 8; 389; 556; 916; 1628; 1696; 1899; 2079; 2249; 2252; 2507; 2685; 3303; 3373; 3382; 3720; 4150; 4233; 4240; 5016; 5280; 5403; 5558; 5650; 5905; 6031; 6130; 6474; 6918; and 6973. A zinc binding region 2 site within SEQ ID NOS: 7235-7244 is identified at amino acid residues 2102-2112 (SEQ JD NO: 7254 HGIAAINSVPW). The polypeptide of SEQ ID NOS: 7235-7244 will be processed by the SARS virus into multiple peptides. This zinc binding region falls within the nspl region of the polypeptide. SEQ ID NO: 7254 is a target for screening of chemical inhibitors to the SARS virus. The invention includes a polypeptide comprises SEQ JD NO: 7254. The invention includes a polynucleotide encoding the polypeptide sequence of SEQ ID NO: 7254. The invention includes a method of screening SEQ ID NO: 7254 for an inhibitor. The invention includes the recombinant expression of SEQ ID NO: 7254 in a host cell. The invention includes a fragment of SEQ JD NOS: 7235-7244, wherein said fragment comprises SEQ JD NO: 7254. The invention includes a polypeptide comprising SEQ ID NO: 7254 wherein said polypeptide is complexed with a zinc ion. The invention includes a small molecule which prevents a zinc ion from complexing with the polypeptide of SEQ ID NO: 7254. The invention includes a fusion protein wherein said fusion protein comprises SEQ ID NO: 7254. The polyprotein encoded by the SARS virus will contain at least two protease domains: a papain-like cystein protease (PLP) and a chymotrypsin-picornavirus 3C-like protease (3CLp). (There may be more than one copy of the PLP domain). These proteases function to cleave the polyprotein into multiple smaller proteins. The 3C-like protease, also known as the "main protease" or Mpro, is itself cleaved from the polyprotein by its own autoprotease activity. See generally, Chapter 35 of Fields Virology (2nd ed), Fields et al. (eds.), B.N. Raven Press, New York, NY, and Anand et al, EMBO Journal (2002) 21 (13): 3213-3224. This 3CLp generally corresponds with the Nsp2 region identified above. The SARS virus 3CLp protein is further characterized by SEQ JD NO: 6569 (also SEQ ID NO: 9769), as shown in FIGURE 15. FIGURE 16 also illustrates the SARS virus 3CLp, in allignment with the 3CLp of avian infectious bronchitis (JBV; SEQ ID NO: 6570), mouse hepatitis virus (MHV; SEQ JD NO: 6571), and bovine coronavirus (BCoV; SEQ ID NO: 6572). Accordingly, the invention includes a polypeptide sequence comprising SEQ ID NO: 6569, or a fragment thereof, or a polypeptide sequence having sequence identity thereto. The invention further includes a polynucleotide sequence encoding SEQ ID NO: 6569, or a fragment thereof. The invention includes a polynucleotide sequence encoding a polypeptide sequence having sequence identity to SEQ JD NO: 6569. The invention further includes a method of screening for an inhibitor of the SARS virus 3CLp protein. In one embodiment, the invention includes a method of screening for an inhibitor of SEQ JD NO: 6569. The invention includes a method of recombinantly expressing the SARS virus 3CLp protein in a host cell. The invention includes a method of recombinantly expressing a polypeptide sequence comprising SEQ ID NO: 6569 or an enzymatically active fragment thereof or a polypeptide sequence having sequence identity thereto. The invention includes a small molecule which inhibits or reduces the proteolytic activity of the SARS virus 3CLp protein. The invention includes a small molecule which inhibits or reduced the proteolytic activity of the polypeptide comprising SEQ ID NO: 6569. Catalytic residues of the SARS virus 3CLp are identified in FIGURE 15 and 16. Specifically, a catalytic histidine and a catalytic cysteine are identified. Such catalytic sites are targets for small molecules which could inhibit or reduce the protease activity of 3CLp. Accordingly, the invention includes a polypeptide comprising a fragment of SEQ ID NO: 6569, wherein said fragment comprises at least one catalytic site. Preferably, the catalytic site is selected from the group consisting of the indicated catalytic histidine and the catalytic cysteine in FIGURE 15 and 16. The invention includes a polynucleotide encoding a polypeptide, wherein said polypeptide comprises a fragment of SEQ JD NO: 6569, wherein said fragment comprises at least one catalytic site. Preferably, the catalytic site is selected from the group consisting of the indicated catalytic histidine and the catalytic cysteine. The invention further includes a method of screening a compound library to identify a small molecule which inhbits a catalytic site of a SARS virus 3CLp. Preferably, the 3CLp comprises SEQ JD NO: 6569, or a fragment thereof, or a sequence having sequence identity thereto. The catalytic site is preferably selected from the group consisting of the indicated catalytic histidine and the catalytic cysteine in FIGURE 15 and 16. The invention includes a small molecule which inhibits the catalytic site of a SARS virus 3CLp. Preferably, the 3CLp comprises SEQ JD NO: 6569, or a fragment thereof, or a sequence having sequence identity thereto. The catalytic site is preferably selected from the group consisting of the indicated catalytic histidine and the catalytic cysteine in FIGURE 15 and 16. Residues of the substrate site of the SARS virus 3CLp are identified in FIGURE 15 and 16. Specifically, a substrate site is indicated at a phenylalanine, a tyrosine and a histidine. Such substrate sites are targets for small molecules which could inhibit or reduce the protease activity of 3CLp. Accordingly, the invention includes a polypeptide comprising a fragment of SEQ JD NO: 6569, wherein said fragment comprises at least one substrate site. Preferably, the substrate site is selected from the group consisting of the indicated substrate phenylalanine, tyrosine and histidine in FIGURE 15 and 16. The invention includes a polynucleotide encoding a polypeptide, wherein said polypeptide comprises a fragment of SEQ ID NO: 6569, wherein said fragment comprises at least one substrate site. Preferably, the substrate site is selected from the group consisting of the indicated substrate phenylalanine, tyrosine and histidine in FIGURE 15 and 16. The invention further includes a method of screening a compound library to identify a small molecule which blocks a subsfrate site of a SARS virus 3CLp. Preferably, the 3CLp comprises SEQ ID NO: 6569, or a fragment thereof, or a sequence having sequence identity thereto. The substrate site is preferably selected from the group consisting of the indicated substrate phenylalanine, tyrosine and histidine in FIGURE 15 and 16. The invention includes a small molecule which inhibits the subsfrate site of a SARS virus 3CLp. Preferably, the 3CLp comprises SEQ ID NO: 6569, or a fragment thereof, or a sequence having sequence identity thereto. The substrate site is preferably selected from the group consisting of the indicated substrate phenylalanine, tyrosine and histidine in FIGURE 15 and 16. The invention further includes a diagnostic kit comprising a polynucleotide encoding a SARS virus 3CLp or a fragment thereof. Preferably, the SARS virus 3CLp comprising SEQ ID NO: 6569 or a fragment thereof or a polypeptide sequence having sequence identity thereto. Preferably, the fragment comprising one or more sites selected from the group consisting of a catalytic site and a substrate site. Preferably, the catalytic site is selected from the group consisting of one or more of the sites identified in FIGURE 15 and 16. Preferably, the substrate site is selected from the group consisting of one or more of the sites identified in FIGURE 15 and 16. The invention further comprises a diagnostic kit comprising an antibody specific to a SARS virus 3CLp or a fragment thereof. Preferably, the antibody is specific to the polypeptide comprising SEQ JD NO: 6569 or a fragment thereof or a polypeptide sequence having sequence identity thereto. Preferably, the antibody is specific to one or more sites of a SARS virus 3CLp selected from the group consisting of a catalytic site and a substrate site. Preferably, the catalytic site is selected from the group consisting of one or more of the sites identified in FIGURE 15 and 16. Preferably, the substrate site is selected from the group consisting of one or more of the sites identified in FIGURE 15 and 16. The invention includes a polypeptide comprising an amino acid sequence from the sequence shown in Figure 25. The two amino acid sequences within Figure 25, separated by a *, are SEQ ID NOS: 7188 & 7189. The invention includes a polypeptide comprising an amino acid sequence having sequence identity to the figure 25 translation. The invention includes a fragment of a polypeptide comprising the figure 25 sequence. The invention includes a diagnostic kit comprising a polypeptide comprising the figure 25 translation, or a fragment thereof. The invention includes a diagnostic kit comprising a polynucleotide sequence encoding the figure 25 translation, or a fragment thereof. The invention includes an immunogenic composition comprising a polypeptide comprising the figure 25 translation, or a fragment thereof. The invention includes an antibody which recognizes a polypeptide comprising the figure 25 sequence, or a fragment thereof. The figure 25 sequence demonstrates functional homology with ORFlb of coronaviruses. SEQ JD NO: 7188 is an open reading frame within Figure 25. The invention includes a polypeptide comprising SEQ ID NO: 7188. The invention includes a polypeptide comprising an amino acid sequence having sequence identity to SEQ ID NO: 7188. The invention includes a fragment of a polypeptide comprising SEQ JD NO: 7188. The invention includes a diagnostic kit comprising a polypeptide comprising SEQ ID NO: 7188, or a fragment thereof. The invention includes a diagnostic kit comprising a polynucleotide sequence encoding SEQ ID NO: 7188, or a fragment thereof. The invention includes an immunogenic composition comprising a polypeptide comprising SEQ JD NO: 7188, or a fragment thereof. The invention includes an antibody which recognizes a polypeptide comprising SEQ ID NO: 7188, or a fragment thereof. SEQ JD NO: 7190 is an open reading frame within SEQ JD NO: 7188. The invention includes a polypeptide comprising SEQ ID NO: 7190, a fragment thereof or a polypeptide having sequence identity thereto. The invention further includes a polynucleotide encoding SEQ ID NO: 7190, a fragment thereof or a polypeptide sequence having sequence identity thereto. An example of a polynucleotide encoding SEQ JD NO: 7190 is given as SEQ JD NO: 7191. SEQ JD NO: 7188 also contains an open reading frame comprising SEQ JD NO: 6042. The invention includes a polypeptide comprising SEQ ID NO: 6042. The invention includes a polypeptide comprising an amino acid sequence having sequence identity to SEQ JD NO: 6042. The invention includes a fragment of a polypeptide comprising SEQ JD NO: 6042. The invention includes a diagnostic kit comprising a polypeptide comprising SEQ JD NO: 6042, or a fragment thereof. The invention includes a diagnostic kit comprising a polynucleotide sequence encoding SEQ JD NO: 6042, or a fragment thereof. The invention includes an immunogenic composition comprising a polypeptide comprising SEQ JD NO: 6042, or a fragment thereof. The invention includes an antibody which recognizes a polypeptide comprising SEQ ID NO: 6042, or a fragment thereof. SEQ ID NO: 6042 demonstrates functional homology to a coronavirus spike protein. Predicted transmembrane regions of SEQ JD NO: 6042 are identified below. Predicted Transmembrane helices of SEQ ID NO: 6042 The sequence positions in brackets denominate the core region . Only scores above 500 are considered significant . Inside to outside helices : 18 found Outside to Lnside helices : 13 found from to score center from to score center 1 ( 1) 16 ( 16) 959 9 1 ( 1) 17 ( 17) 684 10 233 ( 237) 257 ( 252) 905 244 222 ( 222) 240 ( 237) 238 229 345 ( 347) 364 ( 361) 490 354 244 ( 247) 264 ( 264) 613 254 345 ( 354) 369 ( 369) 420 362 349 ( 355) 369 ( 369) 314 362 497 ( 497) 513 ( 513) 239 506 496 ( 496) 511 ( 511) 488 503 573 ( 573) 588 ( 588) 811 580 573 ( 573) 591 ( 591) 712 581 645 ( 648) 666 ( 663) 302 656 650 ( 652) 666 ( 666) 474 659 690 ( 696) 714 ( 711) 428 704 674 ( 679) 702 ( 696) 190 686 857 ( 860) 882 ( 874) 1508 867 ' 691 ( 696) 713 ( 711) 210 704 1031 (1031)1046 (1046) 446 1039 866 ( 868) 886 ( 886) 1172 876 1199 (1203)1219 (1217) 2667 1210 1198 (1201)1215 ( 1215) 3221 1208 SEQ ID NO: 6042, the spike protein, is a surface exposed polypeptide. Recombinant expression of a protein can be hindered by hydrophobic transmembrane regions. Accordingly, the invention includes a polypeptide comprising SEQ ID NO: 6042 wherein one or more of the hydrophobic regions identified above is removed. The invention further includes a polynucleotide encoding such a polypeptide. The invention includes recombinantly expressing the protein in a host cell. Primers for amplifying the gene for spike protein and fragments thereof, such as fragments encoding the soluble ectodomain, include SEQ JD NOS: 9753-9763 (Xiao et al. (2003) Biochem Biophys Res Comm 312:1159-1164). Further characterization of SEQ JD NO: 6042 is set forth below. PSORT Prediction of Protein Localization Sites version 6.4 (WWW) SEQ ID NO: 6042 - 1255 Residues Species classification: 4 *** Reasoning Step: 1 Preliminary Calculation of A OM (threshold: 0.5) count : 2 Position of the most N-terminal TMS: 496 at i=2 MTOP: membrane topology (Hartmann et al . ) I (middle): 503 Charge diffirence (C-N) : 1.0 McG: Examining signal sequence (McGeoch) Length of UR: 13 Peak Value of UR: 3.28 Net Charge of CR: 0 Discriminant Score: 8.66 GvH: Examining signal sequence (von Heijne) Signal Score (-3.5): 5.94 Possible cleavage site: 13 »> Seems to have a cleavable N-term signal seq. Amino Acid Composition of Predicted Mature Form: calculated from 14 ALOM new cnt : 1 ** thrshld changed to -2 Cleavable signal was detected in ALOM?: 0B ALOM: finding transmembrane regions (Klein et al . ) count: 1 value: -12.26 threshold: -2.0 INTEGRAL Likelihood =-12.26 Transmembrane 1202-1218 (1194-1228) PERIPHERAL Likelihood = 0.16 modified ALOM score: 2.55 >» Seems to be a Type la membrane protein The cytoplasmic tail is from 1219 to 1255 (37 Residues) Rule: vesicular pathway Rule: vesicular pathway Rule: vesicular pathway (14) or uncleavable? Gavel: Examining the boundary of mitochondrial targeting seq. motif at: 14 Uncleavable? Ipos set to: 24 ■ Discrimination of mitochondrial target seq. : positive ( 2.18) Rule: vesicular pathway Rule: vesicular pathway Rule: vesicular pathway *** Reasoning Step: 2 KDEL Count : 0 Checking apolar signal for intramitochondrial sorting (Gavel position 24) from: 1 to: 10 Score: 8.0 SKL motif (signal for peroxisomal protein) : pos: 964(1255), count: 1 SRL SKL score (peroxisome): 0.1 Amino Acid Composition Tendency for Peroxisome: 1.37 AAC not from the N-term. , score modified Peroxisomal proteins? Status: notclr AAC score (peroxisome): 0.079 Amino Acid Composition tendency for lysosomal proteins score: 0.39 Status: notclr GY motif in the tail of typela? (lysosomal) Checking the amount of Basic Residues (nucleus) Checking the 4 residue pattern for Nuclear Targeting Checking the 7 residue pattern for Nuclear Targeting Checking the Robbins & Dingwall consensus (nucleus) Checking the RNA binding motif (nucleus or cytoplasm) Nuclear Signal Status: negative ( 0.00) Type la is favored for plasma memb. proteins Checking the NPXY motif.. Checking the YXRF motif.. Checking N-myristoylation.. Final Results plasma membrane Certainty= 0.460 (Affirmative) < suco miσrobody (peroxisome) Certainty= 0.171 (Affirmative) < suco endoplasmic retiσulum (membrane) Certainty= 0.100 (Affirmative) < suco endoplasmic reticulum (lumen) Certainty= 0.100 (Affirmative) < suco SEQ JD NO: 6042 appears to have a N-terminus signaling region, followed by a surface exposed region, followed by a transmembrane region followed by a C-terminus cytoplasmic domain region. Accordingly, the invention includes an immunogenic, surface exposed fragment of SEQ ID NO: 6042. Preferably, said fragment comprises an amino acid sequence which does not include the last 50 amino acids of the C-terminus of SEQ JD NO: 6042. Preferably, said fragment comprises an amino acid sequence which does not include the last 70 amino acids of the C-terminus of SEQ JD NO: 6042. Preferably, said fragment does not include a transdomain region of SEQ JD NO: 6042. Preferably, said fragment does not include a C-terminus cytoplasmic domain of SEQ ID NO: 6042. Preferably, said fragment does not include a N- terminus signal sequence. Preferably, said fragment does not include amino acids 1-10 of the N- terminus of SEQ ID NO: 6042. Preferably, said fragment does not include amino acids 1-14 of the N-terminus of SEQ ID NO: 6042. Two oligopeptide fragments of SEQ JD NO: 6042 that are able to elicit anti-spike antibodies are SEQ ID NOS: 7398 & 7399, as described (with additional C-terminus cysteines) by Xiao et al. (2003) Biochem Biophys Res Comm 312:1159-1164. C-terminal truncations of spike protein, with removal of part of the cytoplasmic region, or removal upto and including the transmembrane region, are described by Yang et al. (2004) Nature 428:561-564. A variant of SEQ ID NO: 6042 that is included within the invention is SEQ ID NO: 9962. Compared to SEQ ID NO: 6042, this sequence has Ser at residue 581 instead of Ala, and has Phe at residue 1152 instead of Leu. The spike protein of coronaviruses may be cleaved into two separate chains into SI and S2. The chains may remain associated together to form a dimer or a trimer. Accordingly, the invention includes a polypeptide comprising SEQ JD NO: 6042 wherein said polypeptide has been cleaved into SI and S2 domains. The invention further includes a polypeptide comprising SEQ ID NO: 6042 wherein amino acids 1-10, preferably amino acids 1-14 of the N-terminus are removed and further wherein SEQ ID NO: 6042 is cleaved into SI and S2 domains. Preferably the polypeptide is in the form of a trimer. The spike protein appears to form an alpha-helical structure in the transmembrane region of the protein, preferably in the S2 domain. This alpha-helical structure is thought to associate with at least two additional spike proteins to form a trimer. Helical or coiled regions of the spike protein are identified below. Predicted coiled-coils of SEQ ID NO: 6042 (spike protein) are at amino acids 900-1005 and 1151-1185 (see Figure 12). Accordingly, the invention comprises a polypeptide sequence comprising a fragment of SEQ ID NO: 6042 wherein said fragment includes a coiled region of SEQ ID NO: 6042. Said fragment preferably includes the amino acid sequences selected from the group consisting of amino acid positions 900 to 1005 and amino acid positions 1151 to 1185 of SEQ JD NO: 6042. The invention comprises a polypeptide sequence comprising a fragment of SEQ JD NO: 6042, wherein said fragment does not include a coiled region of SEQ JD NO: 6042. Said fragment preferably includes the amino acid sequences selected from the group consisting of amino acid positions 900 to 1005 and amino acid positions 1151 and 1185 of SEQ JD NO: 6042. The spike protein is believed to play an integral role in fusion and infection of Coronaviruses with mammalian host cells. Analysis of coronavirus spike proteins as well as similar surface proteins in other viruses has identified at least two structural motifs, typically located within the S2 domain, associated with this fusion event: heptad repeats (HR) and membrane fusion peptides. At least two 4,3 hydrophobic heptad repeat (HR) domains are typically found in the ectodomain of the S2 domain of Coronaviruses. One heptad repeat region (HRl) is typically located adjacent to a fusion peptide while a second heptad region (HR2) is typically located near the C-terminus of the S2 domain, close to the transmembrane anchor. Heptad repeats are characteristic of coiled-coil structures and the heptad repeats found in viral surface proteins (such as coronavirus spike protein) are thought to form bundled helix structures which are involved in viral entry. See Bosch et al, J. Virology (2003) 77:8801-8811 (Figure IB of this reference illustrates an alignment of the HRl and HR2 regions of five coronaviruses along with SARS, annotated "HCov-SARS"). Heptad repeats generally contain a repeating structure of seven amino acids, designated a- b-c-d-e-f-g, where hydrophobic sidechains of residues a and d typically form an apolar stripe, and electrostatic interactions are found in residues e and g. Position a is most frequently Leu, He or Ala and position d is usually Leu or Ala. Residues e and g are often Glu or Gin, with Arg and Lys also prominent at position g. Charged residues are common to positions b, c and/ as these residues may be in contact with solvent. Exceptions to these general parameters are known. For instance Pro residues are sometimes found within the heptad. The HRl and HR2 sequences of an MHV strain have been postulated to assemble into a thermostable, oligomeric, alphahelical rold-like complex, with the HRl and HR2 helices oriented in an antiparallel manner. Id. In this same study, HR2 was asserted to be a strong inhitibor of both virus entry into the cell and cell-cell fusion. HRl and HR2 sequences have been identified in the SARS virus genome. The SARS virus HRl region comprises approximately amino acids 879 to 1005 of SEQ JD NO: 6042 or fragments thereof capable of forming at least one alpha-helical turn. Preferably, said fragments comprise at least 7 (e.g., at least 14, 21, 28, 35, 42, 49 or 56) amino acid residues. SEQ JD NO: 7192, includes amino acids 879 to 1005 of SEQ JD NO: 6042. A preferred fragment of HRl comprises amino acid residues 879 to 980 of SEQ JD NO: 6042. This preferred fragment is SEQ ID NO: 7193. Another preferred fragment of HRl comprises amino acid residues 901 to 1005 of SEQ ID NO: 6042. This preferred fragment is SEQ ID NO: 7194. The SARS virus HR2 region comprises approximately amino acids 1144 to 1201 of SEQ ID NO: 6042, or fragments thereof capable of forming at least one alpha-helical turn. Preferably, said fragments comprise at least 7 (e.g., at least 14, 21, 28, 35, 42, 49 or 56) amino acid residues. SEQ ID NO: 7195 includes amino acids 1144 to 1201. A preferred fragment of HR2 comprises amino acids 1144 to 1195 of SEQ ID NO: 6042. This preferred fragment is SEQ JD NO: 7196. Membrane Fusion peptides sequences within the spike protein are also believed to participate in fusion (and infection) of the virus with a host cell. Fusion peptides generally comprise about 16 to 26 amino acid residues which are conserved within viral families. These Membrane Fusion peptides are relatively hydrophobic and generally show an asymmetric distribution of hydrophobitiy when modeled into an alpha helix. They are also generally rich in alanine and glycine. At least three hydrophobic Membrane Fusion peptide regions have been identified within coronaviruses (PEP1, PEP2, and PEP3). See, Luo et al, "Roles in Cell-Cell Fusion of Two Conserved Hydrophobic Regions in the Murine Coronavirus Spike Protein", Virology (1998) 244:483-494. Figure 1 of this paper shows an alignment of Membrane Fusion peptide sequences of Mouse Hepatitis Viris, Bovine Corona Virus, Feline Infectious Peritonitis Virus, Transmissible Gastroenteritis Virus and Infectious Bronchitis Virus. See also, Bosch et al, "The Coronavirus Spike Protein is a Class I Virus Fusion Protein: Structural and Functional Characterization of the Fusion Core Complex" Journal of Virology (2003) 77(16):8801-8811. PEP1 (SEQ JD NO: 7197), PEP2 (SEQ ID NO: 7198) and PEP3 (SEQ ID NO: 7199) sequences within the SARS spike protein have been identified. The coronavirus spike proteins (and other similar surface viral proteins) are thought to undergo a conformational change upon receptor binding to the target cell membrane. One or more of the hydrophobic Membrane Fusion peptides are thought to become exposed and inserted into the target membrane as a result of this conformational change. The free energy released upon subsequent refolding of the spike protein to its most stable conformation is believed to play a role in the merger of the viral and cellular membranes. One or more SARS HR sequences, preferably HR2, or a fragment thereof may be used to inhibit viral entry and membrane fusion with a target mammalian host cell. The invention provides a method of inhibiting viral infection comprising administering a composition comprising one or more SARS HR polypeptides or a fragment thereof. Preferably, the composition comprises a SARS HR2 sequence. In another embodiment, the invention includes a composition comprising a SARS HRl sequence, or a fragment thereof and a SARS HR2 sequence, or a fragment thereof. The HRl and HR2 sequences may optionally be associated together in an oligomer. The composition may comprise the intermediate domain sequence between the HRl and HR2 domains. The use of such an intermediate sequence may facilitate oligomerization or other structural interaction between the HR regions. HR sequences for use in the invention may be produced recombinantly by methods known in the art. The SARS HR sequences may be modified to facilitate bacterial expression. In particular, the HR sequences may be modified to facilitate transport of the recombinant protein to the surface of the bacterial host cell. For example, leader sequences to a bacterial membrane protein may be added to the N terminus of the recombinant HR sequences. HR sequences for use in the invention may alternatively be produced by chemical synthesis by methods known in the art (see below). As discussed in more detail later in the specification, Applicants have identified structural similarities between the SARS spike protein and the surface protein of Neisseria meningitidis, NadA (and other similar bacterial adhesion proteins). Another means of facilitating bacterial expression of HR sequences includes the addition of the stalk and/or anchor sequences of a NadA-like protein to the C-terminus of the recombinant HR sequences. Recombinant sequences containing the bacterial anchor sequence may preferably be prepared in outer membrane vesicles (the preparation of which is discussed in more detail later in the application). Recombinant sequences missing the bacterial anchor sequences may be secreted and isolated from the supernatant. The invention includes a polypeptide sequence comprising a first sequence and a second sequence, wherein said first sequence comprises a leader sequence for a bacterial membrane protein and wherein said second sequence comprises a HR sequence of a coronavirus. Preferably, said first sequence comprises the leader sequence for a bacterial adhesin protein. More preferably, said bacterial adhesion protein is NadA. Preferably said second sequence comprises HRl, HR2 or both. In one embodiment, the second sequence comprises HRl, HR2 and the intermediate domain sequence present in the naturally occrding spike protein. For example, the second sequence may comprise a fragment of a coronavirus spike protein comprising the amino acids starting with the N-terminus of the HRl region and ending with the C-terminus of the HR2 region. The invention further includes a polypeptide sequence comprising a first, second, third and fourth sequence, wherein the first sequence comprises a leader sequence for a bacterial membrane protein; wherein said second sequence comprises a HR sequence of a coronavirus; wherein said third sequence comprises a stalk domain of a bacterial adhesion protein; and wherein said fourth sequence comprises an anchor domain of a bacterial adhesion protein. In one embodiment, the first sequence comprising the leader peptide sequence is removed. In another embodiment, the third sequence comprising the stalk domain is removed. In another embodiment, the fourth sequence comprising the anchor domain is removed. The polypeptide sequences of the above described constructs may be linked together by means known in the art, including, for example, via glycine linkers. Examples of constructs which may be used in such bacterial expression systems are shown in FIGURE 50. Polypeptide sequences of each of the constructs illustrated in FIGURE 50 are given as SEQ JD NOS : 7200 to 7206. 7200 Leader NadA (1-29) - HRl (879-980) - 6Xgly - HR2 (1144-1195) - stalk+anchor NadA (88-405) 7201 Leader NadA (1-29) - HRl (879-980) - 6Xgly - HR2 (1144-1196) - stalk NadA (88-351) 7202 Leader NadA (1-29) - HRl - HR2 (879-1196) - stalk+anchor NadA (88-405) 7203 Leader NadA (1-29) - HRl - HR2 (879-1196)-stalk NadA (88-351) 7204 HRl - HR2 (879-1196)-stalk NadA (88-35 l)-6xhis 7205 Leader NadA (1-29) - HRl - HR2 (879-1196)-anchor NadA (351-405) 7206 Leader NadA (1-29) - HRl - HR2 (879-1196) Administration of one of more of these Membrane Fusion sequences may also interfere with the ability of a coronavirus to fuse to a host cell membrane. Accordingly, the invention includes an isolated polypeptide comprising an amino acid sequence selected from the group consisting of SEQ JD NO: 7197, SEQ ID NO: 7198and SEQ JD NO: 7199. The invention further includes an isolated polypeptide comprising an amino acid sequence having sequence homology to an amino acid sequence selected from the group consisting of SEQ ID NO: 7197, SEQ ID NO: 7198and SEQ ID NO: 7199. Two or more of these SARS Membrane Fusion peptides can be combined together. The invention includes a composition comprising two SARS Membrane Fusion peptides wherein said peptides are selected from at least two of the amino acids selected from the group consisting of SEQ JD NO: 7197, SEQ JD NO: 7198and SEQ ID NO: 7199, or a sequence having sequence identity thereto. Two or more of the SARS Membrane Fusion peptides may be linked together. Accordingly, the invention includes a polypeptide comprising a first amino acid sequence and a second amino acid sequence, wherein said first and second amino acid sequences are selected from the group consisting of SEQ JD NO: 7197, SEQ ID NO: 7198and SEQ JD NO: 7199, or a sequence having sequence identity thereto. Preferably, said first amino acid sequence and said second amino acid sequence are different SARS Membrane Fusion peptides, i.e., they are not the same. The invention also includes a method of treating or preventing SARS virus infection comprising administering one or more of the SARS Membrane Fusion peptide compositions described above. As discussed above, the spike protein is capable of forming trimers. The invention further includes a polypeptide comprising SEQ JD NO: 6042 in trimeric form. The invention includes a composition comprising at least polypeptides wherein each polypeptide comprises at least the alpha-helical coiled region of a SARS virus spike protein. Preferably, the spike protein comprises SEQ ID NO: 6042 or a fragment thereof. The invention further includes a composition comprising a SARS virus spike protein or a fragment thereof wherein said protein is associated with a transmembrane and wherein said fragment comprises the alpha-helical region of the SARS virus spike protein. Preferably, the composition comprises at least three SARS virus spike proteins or a fragment thereof, wherein the fragment comprises the alpha-helical region of the SARS virus spike protein. The invention further includes an antibody which specifically binds to a trimeric form of SARS virus spike proteins. Preferably, the spike protein comprises SEQ ID NO: 6042 or a fragment thereof. The invention includes an antibody which specifically binds to a trimeric form of SARS virus spike proteins wherein said proteins are associated with a transmembrane. The invention further includes an antibody which specifically binds to a monomeric form of SARS virus spike protein or a fragment thereof. Preferably, the antibody specifically binds to a monomeric form of SEQ JD NO: 6042 or a fragment thereof. The invention further includes a small molecule which interferes with or disrupts the coiling of a SARS viral spike protein trimer. The invention further includes an attenuated SARS virus for use as a vaccine wherein said attenuated virus contains a polynucleotide insertion, deletion or substitution which does not disrupt the trimeric conformation of the SARS virus spike protein. The invention further includes an attenuated SARS virus for use as a vaccine wherein said attenuated virus contains a polynucleotide insertion, deletion or substitution which does not disrupt the alpha-helical formation of the SARS virus spike protein. The spike protein may be recombinantly produced. In one embodiment, the spike protein is expressed in virus like particles so that the protein is attached to a cell membrane. Such attachment may facilitate presentation of immunogenic epitopes of the spike protein. Preferably, the alpha-helical portion of the spike protein is associated with the cell membrane. Preferably, the spike proteins form a trimer within the transmembrane region of attachment. Predicted N-glycosylation sites of SEQ JD NO: 6042 are identified below: Position Pot ;entia_ Jury NGlyc agreement result 29 NYTQ SEQ ID NO: 7207 0 .7751 (9/9) +++ 65 NVTG SEQ ID NO: 7208 0 .8090 (9/9) +++ 109 NKSQ SEQ ID NO: 7209 0, .6081 (7/9) + 119 NSTN SEQ ID NO: 7210 0 .7039 (9/9) ++ 158 NCTF SEQ ID NO: 7211 0, .5808 (7/9) + 227 NITN SEQ ID NO: 7212 0 .7518 (9/9) +++ 269 NGTI SEQ ID NO: 7213 0. .6910 (9/9) ++ 318 NITN SEQ ID NO: 7214 0 .6414 (9/9) ++ 330 NATK SEQ ID NO: 7215 0, .6063 (8/9) + 357 NSTF SEQ ID NO: 7216 0. .5746 (8/9) + 589 NASS SEQ ID NO: 7217 0. .5778 (6/9) + 602 NCTD SEQ ID NO: 7218 0, .6882 (9/9) ++ 699 NFSI SEQ ID NO: 7219 0, .5357 (7/9) + 783 NFSQ SEQ ID NO: 7220 0, .6348 (9/9) ++ 1080 NGTS SEQ ID NO: 7221 0, .5806 (7/9) + 1116 NNTV SEQ ID NO: 7222 0, .5106 (5/9) + 1176 NΞSL SEQ ID NO: 7223 0. .6796 (9/9) ++ Accordingly, the invention includes a polypeptide comprising a fragment of SEQ JD NO: 6042 wherein said fragment comprises one or more of the glycosylation sites identified above (SEQ JD NOS: 7207-7223). The invention further includes a polynucleotide encoding one or more of the fragments identified above. This glycosylation site can be covalently attached to a saccharide. Accordingly, the invention includes a polypeptide comprising a fragment of SEQ ID NO: 6042 wherein said fragment comprises one or more of the glycosylation sites identified above and wherein said polypeptide is glycosylated at one or more of the sites identified above. Predicted O-glycosylation sites are identified below: Residue No. Potential Threshold Assignment Thr 698 0.8922 0.7696 T Thr 706 0.9598 0.7870 T Thr 922 0.9141 0.7338 T Ser 36 0.8906 0.7264 S Ser 703 0.8412 0.7676 S The invention includes a polypeptide comprising a fragment of SEQ JD NO: 6042 wherein said fragment comprises one or more of the O-glycosylation sites identified above. The invention further includes a polynucleotide encoding one or more of the fragments identified above. The invention further includes a polypeptide comprising a fragment of SEQ ID NO: 6042 wherein said fragment comprises one or more of the O-glycosylation sites identified above and further wherein the polypeptide is covalently bonded to a saccharide at one or more of the included glycosylation sites. The invention further includes a polypeptide comprising a fragment of SEQ JD NO: 6042 wherein said fragment comprises one or more of the N-glycosylation sites identified above and further wherein said fragment comprises one or more of the O-glycosylation sites identified above. The invention includes a polypeptide comprising a fragment of SEQ JD NO: 6042 wherein said fragment does not include one or more of the glycosylation sites identified above. The invention also includes a polynucleotide encoding such a polypeptide. Predicted phosphorylation sites of SEQ JD NO: 6042 are Ser-346, Tyr-195, and Tyr-723. Accordingly, the invention comprises a polypeptide comprising a fragment of SEQ ID NO: 6042 wherein said fragment comprises at least ten amino acid residues and wherein said fragment comprises one or more of the amino acids selected from the group consisting of Ser-346, Tyr- 195, and Tyr-723. In one embodiment, one or more of the amino acids selected from the group consisting of Ser-346, Tyr-195, and Tyr-723 are phosphorylated. Expression and functional characterization of the spike glycoprotein has been described by Xiao et al. (2003) Biochem Biophys Res Comm 312:1159-1164. T-epitopes for SEQ JD NO: 6042 are identified in Table 16. The invention includes a polypeptide for use as an antigen, wherein the polypeptide comprises: (a) an amino acid sequence selected from the group consisting of the T-epitope sequences identified as SEQ ID NOS: 8041-8280; (b) an amino acid sequence having sequence identity to an amino acid sequence of (a). The invention further comprising a polynucleotide sequence encoding the polypeptides of (a) or (b). The invention further comprising a method of expression or delivery of such polynucleotides through viral vectors and/or viral particles. The invention further comprises a polypeptide comprising two or more of the T-epitope sequences identified in SEQ ID NOS: 8041-8280, or a polynucleotide encoding such a polypeptide. The use as an antigen is preferably a use: (1) as a T-cell antigen; (2) for generating a complex between a class I MHC protein (e.g. a class I HLA) and a fragment of said antigen; (3) as an antigen for raising a cell-mediated immune response; and/or (4) as an antigen for raising a CTL response. The use preferably protects or treats disease and/or infection caused by a SARS virus. The invention provides the use of a polypeptide in the manufacture of a medicament for immunising a mammal (typically a human) against SARS viral infection wherein the polypeptide is as defined above. The invention provides a method of raising an immune response in a mammal (typically a human), comprising the step of administering to the mammal a polypeptide as defined above, wherein said immune response is a cell-mediated immune response and, preferably, a CTL response. The immune response is preferably protective or therapeutic. The invention includes a polypeptide comprising SEQ ID NO: 6040. The invention includes a polypeptide comprising an amino acid sequence having sequence identity to SEQ JD NO: 6040. The invention includes a fragment of a polypeptide comprising SEQ JD NO: 6040. The invention includes a polynucleotide encoding SEQ JD NO: 6040 or a fragment thereof. The invention includes a diagnostic kit comprising a polypeptide comprising SEQ ID NO: 6040 or a fragment thereof. The invention includes a diagnostic kit comprising a polynucleotide sequence encoding SEQ ID NO: 6040 or a fragment thereof. The invention includes an antibody which recognizes a polypeptide comprising SEQ JD NO: 6040 or a fragment thereof. SEQ JD NO: 6040 demonstrates functional homology with a membrane protein of coronaviruses. Predicted transmembrane helices of SEQ JD NO: 6040 are identified below: Predicted Transmembrane Helices The sequence positions in brackets denominate the core region . Only scores above 500 are considered significant . Inside to outside helices : 3 found from to score center 27 ( 30 ) 48 ( 45 ) 1138 38 137 ( 139 ) 153 ( 153 ) 486 146 Outside to inside helices : 3 found from to score center 28 ( 31 ) 45 ( 45 ) 819 38 71 ( 73 ) 90 ( 90 ) 210 81 136 ( 142 ) 156 ( 156 ) 272 149 The amino acid region with the highest predicted transmembrane helical region is from amino acid position 27 to 48 of SEQ ID NO: 6040. Such transmembrane regions are often difficult to express recombinantly. Accordingly, the invention includes a polypeptide comprising a fragment of SEQ JD NO: 6040 wherein said fragment does not include the amino acid sequence between positions 27 to 48. The invention includes a polypeptide comprising a fragment of SEQ ID NO: 6040 wherein said fragment does not include the amino acid sequence between positions 28 to 45. The invention also includes a polynucleotide sequence encoding any of the above-identified polypeptides. SEQ JD NO: 6040 is predicted to be a hypothetical protein of the SARS virus. A prediction of the protein localization of SEQ ID NO: 6040 is set forth below. SEQ JD NO: 6040 is predicted to be located in one of the following locations: mitochondrial matrix space, microbody (peroxisome), nucleus, and mitochondrial inner membrane. SEQ ID NO: 6040 is predicted to be associated with an organelle inside an infected cell. Accordingly, SEQ JD NO: 6040 is a target for screening of chemical inhibitors to the SARS virus. The invention includes a polypeptide comprises SEQ ID NO: 6040 or a fragment thereof. The invention includes a polynucleotide encoding the polypeptide sequence of SEQ JD NO: 6040 or a fragment thereof. The invention includes a method of screening SEQ JD NO: 6040 for an inhibitor. The invention includes the recombinant expression of SEQ ID NO: 6040 in a host cell. The invention includes a small molecule which prevents the polypeptide of SEQ ID NO: 6040 from associating with an organelle inside of an infected cell. The invention includes a fusion protein wherein said fusion protein comprises SEQ ID NO: 6040. PSORT Prediction of Protein Localization Sites version 6.4 (WWW) SEQ ID NO: 6040 163 Residues Species classification: 4 *** Reasoning Step: 1 Preliminary Calculation of ALOM (threshold: 0.5) count : 0 McG: Examining signal sequence (McGeoch) Length of UR: 9 Peak Value of UR: 1.75 Net Charge of CR: 1 Discriminant Score: -2.56 GvH: Examining signal sequence (von Heijne) Signal Score (-3.5): 1.94 Possible cleavage site: 53 >» Seems to have no N-terminal signal seq. Amino Acid Composition of Predicted Mature Form: calculated from 1 ALOM new cnt: 0 ** thrshld changed to -2 Cleavable signal was detected in ALOM?: OB ALOM: finding transmembrane regions (Klein et al . ) count: 0 value: 1.32 threshold: -2.0 PERIPHERAL Likelihood = 1.32 modified ALOM score: -1.16 Gavel: Examining the boundary of mitochondrial targeting seq. motif at: 156 HRSVTI Discrimination of mitochondrial target seq. : notclr ( 0.88) Rule: mitochondrial protein Rule: mitochondrial protein Rule: mitochondrial protein Rule: mitochondrial protein *** Reasoning Step: 2 KDEL Count : 0 Checking apolar signal for intramitochondrial sorting (Gavel position 156) from: 27 to: 44 Score: 5.0 Mitochondrial matrix? Score: 0.36 SKL motif (signal for peroxisomal protein) : pos: 99(163), count: 1 SKL SKL score (peroxisome): 0.3 Amino Acid Composition Tendency for Peroxisome: -4.28 Peroxisomal proteins? Status: notclr Amino Acid Composition tendency for lysosomal proteins score: 0.02 Status: notclr Modified score for lysosome: 0.152 Checking the amount of Basic Residues (nucleus) Checking the 4 residue pattern for Nuclear Targeting Found: pos: 132 (5) KRKR Checking the 7 residue pattern for Nuclear Targeting Checking the Robbins & Dingwall consensus (nucleus) Checking the RNA binding motif (nucleus or cytoplasm) nuc modified. Score: 0.60 Nuclear Signal Status: notclr ( 0.30) Checking CaaX motif.. Checking N-myristoylation.. Checking CaaX motif .. Final Results mitochondrial matrix space Certainty= 0.480 (Affirmative) < suco microbody (peroxisome) Certainty= 0.300 (Affirmative) < suco nucleus Certainty= 0.300 (Affirmative) < suco mitochondrial inner membrane Certainty= 0.188 (Affirmative) < suco Predicted N-glycosylation sites of SEQ JD NO: 6040 are identified below. Position Potential Jury NGlyc agreement result 2 NKTG (SEQ ID NO: 7255) 0.7804 (9/9) +++ 106 NLTL (SEQ ID NO: 7256) 0.6123 (7/9) + Accordingly, the invention comprises a fragment of SEQ ID NO: 6040 wherein said fragment is at least ten amino acids and wherein said fragment comprises one or more of the asparagines from the amino acid positions of SEQ ID NO: 6040 selected from the group consisting of 2 and 106. The invention includes a fragment of SEQ ID NO: 6040 wherein said fragment comprises one or more amino acid sequences selected from the group consisting of SEQ JD NO: 7255 and SEQ ID NO: 7256. Preferably, the fragment comprises the amino acid sequence NKTG (SEQ ID NO: 7255). The invention includes a polypeptide comprising a fragment of SEQ JD NO: 6040 wherein said fragment does not include one or more of the glycosylation sites identified above. The invention also includes a polynucleotide encoding such a polypeptide. T-epitopes for SEQ ID NO: 6040 are identified in Table 14. The invention includes a polypeptide for use as an antigen, wherein the polypeptide comprises: (a) an amino acid sequence selected from the group consisting of the T-epitope sequences identified in SEQ ID NOS: 7640-7800; (b) an amino acid sequence having sequence identity to an amino acid sequence of (a). The invention further comprising a polynucleotide sequence encoding the polypeptides of (a) or (b). The invention further comprising a method of expression or delivery of such polynucleotides through viral vectors and/or viral particles. The invention further comprises a polypeptide comprising two or more of the T-epitope sequences identified in SEQ ID NOS: 7640-7800, or a polynucleotide encoding such a polypeptide. The use as an antigen is preferably a use: (1) as a T-cell antigen; (2) for generating a complex between a class I MHC protein (e.g. a class I HLA) and a fragment of said antigen; (3) as an antigen for raising a cell-mediated immune response; and/or (4) as an antigen for raising a CTL response. The use preferably protects or treats disease and/or infection caused by a SARS virus. The invention provides the use of a polypeptide in the manufacture of a medicament for immunising a mammal (typically a human) against SARS viral infection wherein the polypeptide is as defined above. The invention provides a method of raising an immune response in a mammal (typically a human), comprising the step of administering to the mammal a polypeptide as defined above, wherein said immune response is a cell-mediated immune response and, preferably, a CTL response. The immune response is preferably protective or therapeutic. The invention includes a polypeptide comprising SEQ ID NO: 6041. SEQ LD NO: 6041 demonstrates functional homology with a portion of an ORF lab polyprotein. The invention includes a polypeptide comprising an amino acid sequence having sequence identity to SEQ JD NO: 6041. The invention includes a fragment of a polypeptide comprising SEQ ID NO: 6041. The invention includes a polynucleotide sequence encoding an amino acid sequence having sequence identity to SEQ JD NO: 6041. The invention includes a polynucleotide encoding a fragment of a polypeptide comprising SEQ ID NO: 6041. The invention includes a diagnostic kit comprising a polypeptide comprising SEQ JD NO: 6041 or a fragment therof. The invention includes a diagnostic kit comprising a polynucleotide encoding SEQ JD NO: 6041 or a fragment thereof. The invention includes an immunogenic composition comprising a polypeptide comprising SEQ JD NO: 6041 or a fragment thereof. The invention includes an antibody which recognizes a polypeptide comprising SEQ ID NO: 6041 or a fragment thereof. The polyproteins of coronaviruses are associated with enzymatic activity. Accordingly, SEQ JD NO: 6041 is a target for screening of chemical inhibitors to the SARS virus. The invention includes a polypeptide comprising SEQ JD NO: 6041 or a fragment thereof. The invention includes a polynucleotide encoding the polypeptide sequence of SEQ JD NO: 6041 or a fragment thereof. The invention includes a method of screening SEQ JD NO: 6041 for an inhibitor. The invention includes the recombinant expression of SEQ ID NO: 6041 in a host cell. The invention includes a small molecule which prevents the polypeptide of SEQ ID NO: 6041 from performing enzymative activity. The invention includes a fusion protein wherein said fusion protein comprises SEQ JD NO: 6041. Predicted transmembrane or hydrophobic regions of SEQ ID NO: 6041 are identified below. Although the polyprotein of coronaviruses is proteolytically cleaved into numerous smaller proteins, hydrophobic domains in the polyprotein are known to mediate the membrane association of the replication complex and to be able to dramatically alter the architecture of host cell membranes. Accordingly, the hydrophobic domains of the polyprotein are targets for genetic mutation to develop attenuated SARS virus vaccines. The hydrophobic domains are also targets for small molecule inhibitors of the SARS virus. The hydrophobic domains may also be used to generate antibodies specific to those regions to treat or prevent SARS virus infection. Possible transmembrane helices of SEQ ID NO: 6041 The sequence positions in brackets denominate the core region . Only scores above 500 are considered significant . Inside to outside helices : 18 found from to score center 234 ( 234) 254 ( 250) 1046 241 256 ( 256) 272 ( 270) 252 263 319 ( 319) 334 ( 334) 227 327 503 ( 505) 522 ( 519) 405 512 613 ( 615) 633 ( 629) 619 622 677 ( 679) 703 ( 696) 467 689 849 ( 851) 869 ( 865) 229 858 1080 (1080)1097 (1094) 306 1087 1147 (1149)1163 (1163) 354 1156 1557 (1557)1581 (1577) 817 1567 1954 (1954)1971 (1971) 832 1964 2369 (2372)2395 (2387) 300 2379 2513 (2513)2532 (2529) 690 2522 Outsi de to inside helices : 14 found from to score center 239 ( 239) 254 ( 254) 924 247 239 ( 248) 272 ( 263) 468 256 311 ( 314) 334 ( 328) 267 321 499 ( 503) 522 ( 519) 485 512 617 ( 617) 634 ( 631) 425 624 849 ( 853) 872 ( 872) 572 864 1147 (1147)1162 (1162) 765 1155 1564 (1564)1581 (1579) 883 1572 1951 (1951)1968 (1966) 657 1958 2513 (2522)2539 (2537) 711 2529 Accordingly, the invention includes a polypeptide comprising a fragment of SEQ ID NO: 6041, wherein said fragment comprises an amino acid sequence including one or more of the hydrophobic transmembrane sequences identified above. The invention includes a polypeptide comprising a fragment of SEQ ID NO: 6041 wherein said fragment comprises one or more of the following polypeptide sequences of SEQ ID NO: 6041: 234-254, 613-633, 1557-1581, 1954- 1971, 2513-2532, 239-254, 1564-1581, 1951-1968, 2513-2539. Preferably, the fragment comprises one or more of the following polypeptide sequences of SEQ JD NO: 6041 : 234-254 and 239-254. The invention also includes polynucleotides encoding each of the polypeptide fragments identified above. The invention includes an attenuated SARS virus wherein said attenuated SARS virus contains an addition, deletion or substitution in the polynucleotides encoding for one of the hydrophobic domains identified above. The invention also includes a method for creating an attenuated SARS virus comprising mutating a SARS virus by adding, deleting or substituting the viral genome of the SARS virus to alter the coding of one or more of the hydrophobic domains of SEQ ID NO: 6041 identified above. The invention includes an antibody which specifically identifies one or more of the hydrophobic regions of SEQ ID NO: 6041 identified above. The invention includes a small molecule which binds to, interferes with the hydrophobicity of or otherwise disrupts one or more of the hydrophobic regions of SEQ JD NO: 6041 identified above. Predicted N-glycosylation sites of SEQ JD NO: 6041 are identified below: Position Potential Jury NGlyc agreement result 571 NLSH (SEQ ID NO: 7257) 0.6598 (8/9) + 835 NTSR (SEQ ID NO: 7258) 0.5762 (7/9) + 958 NVTD (SEQ ID NO: 7259) 0.7494 (9/9) ++ 1113 NISD (SEQ ID NO: 7260) 0.7259 (8/9) + 1205 NSTL (SEQ ID NO: 7261) 0.6296 (9/9) ++ 1460 NVTG (SEQ ID NO: 7262) 0.6844 (9/9) ++ 1685 NHSV (SEQ ID NO: 7263) 0.5181 (5/9) + 2029 NKTT (SEQ ID NO: 7264) 0.5423 (5/9) + Accordingly, the invention comprises a polypeptide comprising a fragment of the amino acid sequence of SEQ JD NO: 6041, wherein said fragment comprises one or more of the N- glycosylation sites identified above. The invention comprises a polypeptide comprising a fragment of SEQ JD NO: 6041 wherein said fragment comprises one or more of sequences SEQ JD NOS: 7257-7264. Preferably, the fragment comprises one or more of the sequences SEQ JD NOS: 7257, 7259, 7260, 7261 and 7262. The invention further comprises a polynucleotide encoding one or more of the polypeptides identified above. The invention includes a polypeptide comprising a fragment of SEQ JD NO: 6041 wherein said fragment does not include one or more of the glycosylation sites identified above. The invention also includes a polynucleotide encoding such a polypeptide. T-epitopes for SEQ JD NO: 6041 are identified in Table 15. The invention includes a polypeptide for use as an antigen, wherein the polypeptide comprises: (a) an amino acid sequence selected from the group consisting of the T-epitope sequences identified in SEQ JD NOS: 7801-8040; (b) an amino acid sequence having sequence identity to an amino acid sequence of (a). The invention further comprising a polynucleotide sequence encoding the polypeptides of (a) or (b). The invention further comprising a method of expression or delivery of such polynucleotides through viral vectors and/or viral particles. The invention further comprises a polypeptide comprising two or more of the T-epitope sequences identified in SEQ ID NOS: 7801-8040, or a polynucleotide encoding such a polypeptide. The use as an antigen is preferably a use: (1) as a T-cell antigen; (2) for generating a complex between a class I MHC protein (e.g. a class I HLA) and a fragment of said antigen; (3) as an antigen for raising a cell-mediated immune response; and/or (4) as an antigen for raising a CTL response. The use preferably protects or treats disease and/or infection caused by a SARS virus. The invention provides the use of a polypeptide in the manufacture of a medicament for immunising a mammal (typically a human) against SARS viral infection wherein the polypeptide is as defined above. The invention provides a method of raising an immune response in a mammal (typically a human), comprising the step of administering to the mammal a polypeptide as defined above, wherein said immune response is a cell-mediated immune response and, preferably, a CTL response. The immune response is preferably protective or therapeutic. The invention includes a polypeptide sequence SEQ ID NO: 6043 or a fragment thereof. The invention includes a polypeptide comprising an amino acid sequence having sequence identity to SEQ ID NO: 6043. The invention includes a polynucleotide sequence encoding the amino acid sequence of SEQ JD NO: 6043 or a fragment thereof. Predicted transmembrane regions of SEQ JD NO: 6043 are set forth below. Inside to outside helices : 4 found from to score center 41 ( 41 ) 56 ( 56 ) 1789 49 76 ( 79 ) 99 ( 99 ) 2142 89 105 ( 105 ) 125 ( 125 ) 1250 115 Outside to inside helices : 3 found from to score center 41 ( 41) 59 ( 56) 2053 49 76 ( 82) 98 ( 96) 1580 89 103 ( 105) 125 ( 123) 1257 115 The amino acid region with the highest predicted transmembrane helical region is from amino acid position 76 to 99 of SEQ JD NO: 6043. Such transmembrane regions are often difficult to express recombinantly. Accordingly, the invention includes a polypeptide comprising a fragment of SEQ JD NO: 6043 wherein said fragment does not include one or more of the hydrophobic amino acid sequences identified above. Preferably, the fragment does not include the amino acids between positions 27 to 48. The invention also includes a polynucleotide sequence encoding any of the above-identified polypeptides. SEQ JD NO: 6043 is predicted to be a hypothetical protein of the SARS virus. A prediction of the protein localization of SEQ JD NO: 6043 is set forth below. SEQ JD NO: 6043 is predicted to be located in one of the following locations: mitochondrial inner membrane, plasma membrane, Golgi body, and mitochondrial intermembrane space. SEQ ID NO: 6043 may be associated with an organelle inside an infected cell. Accordingly, SEQ JD NO: 6043 is a target for screening of chemical inhibitors to the SARS virus. The invention includes a polypeptide comprises SEQ JD NO: 6043 or a fragment thereof. The invention includes a polynucleotide encoding the polypeptide sequence of SEQ JD NO: 6043 or a fragment thereof. The invention includes a method of screening SEQ ID NO: 6043 for an inhibitor. The invention includes the recombinant expression of SEQ ID NO: 6043 in a host cell. The invention includes a small molecule which prevents the polypeptide of SEQ JD NO: 6043 from associating with an organelle inside of an infected cell. The invention includes a fusion protein wherein said fusion protein comprises SEQ JD NO: 6043. PSORT Prediction of Protein Localization Sites for SEQ ID NO: 6043 version 6.4 (WWW) Species classification: 4 *** Reasoning Step: 1 Preliminary Calculation of ALOM (threshold: 0.5) count : 3 Position of the most N-terminal TMS: 40 at i=2 MTOP: membrane topology (Hartmann et al . ) I (middle): 47 Charge diffirence (C-N) : 3.5 McG: Examining signal sequence (McGeoch) Length of UR: 12 Peak Value of UR: 1.41 Net Charge of CR: 0 Discriminant Score: 1 -4.67 GvH: Examining signal sequence (von Heijne) Signal Score (-3.5): 3.44 Possible cleavage site: 15 >» Seems to have no N-terminal signal seq. Amino Acid Composition of Predicted Mature Form: calculated from 1 ALOM new cnt: 2 ** thrshld changed to -2 Cleavable signal was detected in ALOM? : 0B ALOM: finding transmembrane regions (Klein et al . ) count: 2 value: -6.90 threshold: -2.0 INTEGRAL Likelihood = -6, .90 Transmembrane 83 - 99 ( 78 - - 101) INTEGRAL Likelihood = -5. .04 Transmembrane 40 - 56 ( 37 - - 60) PERIPHERAL Likelihood = -0, .32 modified ALOM score: 1. 48 >» Likely a Type Illb membrane protein (Nexo Ccyt) Gavel: Examining the boundary of mitochondrial targeting seq. motif at: 128 MRCWLC Discrimination of mitochondrial target seq. : notclr ( 0.76) Rule: mitochondrial protein Rule : mitochondrial protein Rule: mitochondrial protein Rule: mitochondrial protein *** Reasoning Step: 2 Type Ilia or Illb is favored for ER memb. proteins KDEL Count: 0 Checking apolar signal for intramitochondrial sorting (Gavel position 128) from: 39 to: 56 Score: 11.5 >» Seems to have an intramitochondrial signal Mitochondrial inner membrane? Score: 0.59 Mitochondrial intermemb. space? Score: 0.22 SKL motif (signal for peroxisomal protein) : pos: 92(274), count: 1 SHL SKL score (peroxisome): 0.3 Amino Acid Composition Tendency for Peroxisome: 4.78 Peroxisomal proteins? Status: positive Amino Acid Composition tendency for lysosomal proteins score: 1.16 Status: notclr Type III proteins may be localized at Golgi Checking the amount of Basic Residues (nucleus) Checking the 4 residue pattern for Nuclear Targeting Checking the 7 residue pattern for Nuclear Targeting Checking the Robbins & Dingwall consensus (nucleus) Checking the RNA binding motif (nucleus or cytoplasm) Nuclear Signal Status: negative ( 0.00) Check the Number of TMSs for typelll (plasma memb. ) Checking N-myristoylation.. Final Results mitochondrial inner membrane Certainty= 0.664(Affirmative) < suco plasma membrane Certainty= 0.600 (Affirmative) < suco Golgi body Certainty= 0.400 (Affirmative) < suco mitochondrial intermembrane space Certainty= 0.362 (Affirmative) < suco Predicted N- and O- glycosylation sites of SEQ ID NO: 6043 are identified below. Position Potential Jury NGlyc agreement result 227 NATF (SEQ ID NO: 7265) 0.6328 (7/9) + Residue No. P Pootteennttiiaal Threshold Assignment T Thhrr 2 288 0. .9095 0, .6280 T T Thhrr 3 322 0. .8740 0. .6595 T Thr 34 0. .9058 0. .6655 T Thr 170 0. .6816 0 .6600 T Thr 267 0, .9240 0 .5779 T Thr 268 0. .7313 0, .5708 T Thr 269 0. .9859 0, .5583 T Thr 270 0. .8023 0, .5492 T Ser 27 0. .6930 0. .6091 s Ser 252 0. .6457 0. .5977 s Accordingly, the invention comprises a polypeptide comprising a fragment of the amino acid sequence of SEQ ID NO: 6043, wherein said fragment comprises the N-glycosylation sites or O-glycosylation sites identified above. The invention comprises a polypeptide comprising a fragment of SEQ JD NO: 6043 wherein said fragment comprises one or more of the N- glycosylation sites or O-glycosylation sites identified above. The invention further comprises a polynucleotide encoding one or more of the polypeptides identified above. The invention includes a polypeptide comprising a fragment of SEQ JD NO: 6043 wherein said fragment does not include one or more of the glycosylation sites identified above. The invention also includes a polynucleotide encoding such a polypeptide. T-epitopes for SEQ JD NO: 6043 are identified in Table 17. The invention includes a polypeptide for use as an antigen, wherein the polypeptide comprises: (a) an amino acid sequence selected from the group consisting of the T-epitope sequences identified in SEQ ID NOS: 8281-8486; (b) an amino acid sequence having sequence identity to an amino acid sequence of (a). The invention further comprising a polynucleotide sequence encoding the polypeptides of (a) or (b). The invention further comprising a method of expression or delivery of such polynucleotides through viral vectors and/or viral particles. The invention further comprises a polypeptide comprising two or more of the T-epitope sequences identified in SEQ ID NOS: 8281-8486, or a polynucleotide encoding such a polypeptide. The use as an antigen is preferably a use: (1) as a T-cell antigen; (2) for generating a complex between a class I MHC protein (e.g. a class I HLA) and a fragment of said antigen; (3) as an antigen for raising a cell-mediated immune response; and/or (4) as an antigen for raising a CTL response. The use preferably protects or treats disease and/or infection caused by a SARS virus. The invention provides the use of a polypeptide in the manufacture of a medicament for immunising a mammal (typically a human) against SARS viral infection wherein the polypeptide is as defined above. The invention provides a method of raising an immune response in a mammal (typically a human), comprising the step of administering to the mammal a polypeptide as defined above, wherein said immune response is a cell-mediated immune response and, preferably, a CTL response. The immune response is preferably protective or therapeutic. The invention includes a polypeptide comprising SEQ JD NO: 6044. The invention includes a polypeptide comprising a fragment of SEQ ID NO: 6044 or a sequence having sequence identity to SEQ JD NO: 206. The invention includes a polynucleotide encoding SEQ JD NO: 6044. SEQ JD NO: 6044 is identified as a hypothetical protein. Predicted hydrophobic or transmembrane regions of SEQ JD NO: 6044 are identified below: Inside to outside helices : 3 found from to score center 1 ( 1) 17 ( 15) 891 8 47 ( 47) 66 ( 63) 221 56 Outside to inside helices : 4 found from to score center 1 ( 4) 21 ( 19) 599 11 Accordingly, the invention includes a polypeptide comprising a fragment of SEQ ID NO: 6044 wherein said fragment does not include one or more of the hydrophobic amino acid sequences identified above. Preferably, the fragment does not include the amino acids between positions 1 to 19. The invention also includes a polynucleotide sequence encoding any of the above-identified polypeptides. SEQ JD NO: 6044 is predicted to be a hypothetical protein of SARS virus. A prediction of the protein localization of SEQ ID NO: 6044 is set forth below. SEQ JD NO: 6044 is predicted to be located in one of the following locations: nucleus, mitochondrial matrix, lysosome (lumen), and microbody (peroxisome). SEQ ID NO: 6044 may be associated with an organelle inside an infected cell. Accordingly, SEQ JD NO: 6044 is a target for screening of chemical inhibitors to the SARS virus. The invention includes a polypeptide comprises SEQ ID NO: 6044 or a fragment thereof. The invention includes a polynucleotide encoding the polypeptide sequence of SEQ JD NO: 6044 or a fragment thereof. The invention includes a method of screening SEQ ID NO: 6044 for an inhibitor. The invention includes the recombinant expression of SEQ JD NO: 6044 in a host cell. The invention includes a small molecule which prevents the polypeptide of SEQ ID NO: 6044 from associating with an organelle inside of an infected cell. The invention includes a fusion protein wherein said fusion protein comprises SEQ ID NO: 6044. PSORT Prediction of Protein Localization Sites for SEQ ID NO : 6044 version 6 .4 (WWW) 154 Residues Species classification: 4 *** Reasoning Step: 1 Preliminary Calculation of ALOM (threshold: 0.5) count: 0 McG: Examining signal sequence (McGeoch) Length of UR: 7 Peak Value of UR: 1.06 Net Charge of CR: 1 Discriminant Score: -7.97 GvH: Examining signal sequence (von Heijne) Signal Score (-3.5): -3.28 Possible cleavage site: 34 >» Seems to have no N-terminal signal seq. Amino Acid Composition of Predicted Mature Form: calculated from 1 ALOM new cnt: 0 ** thrshld changed to -2 Cleavable signal was detected in ALOM? : 0B ALOM: finding transmembrane regions (Klein et al . ) count: 0 value: 1.43 threshold: -2.0 PERIPHERAL Likelihood = 1.43 modified ALOM score: -1.19 Gavel: Examining the boundary of mitochondrial targeting seq. motif at: 151 FRKKQV Discrimination of mitochondrial target seq. : notclr (-0.46) *** Reasoning Step: 2 KDEL Count: 0 Checking apolar signal for intramitochondrial sorting (Gavel position 151) from: 46 to: 50 Score: 5.0 Mitochondrial matrix? Score: 0.36 SKL motif (signal for peroxisomal protein) : pos: -1(154), count: 0 Amino Acid Composition Tendency for Peroxisome: 0.61 Peroxisomal proteins? Status: notclr AAC score (peroxisome): 0.149 Amino Acid Composition tendency for lysosomal proteins score: 0.81 Status: notclr Modified score for lysosome: 0.231 Checking the amount of Basic Residues (nucleus) Checking the 4 residue pattern for Nuclear Targeting Found: pos: 134 (3) KHKK Checking the 7 residue pattern for Nuclear Targeting Checking the Robbins & Dingwall consensus (nucleus) Found: pos: 136 (3) KK VSTNLCTHSF RKKQV Final Robbins Score (nucleus): 0.60 Checking the RNA binding motif (nucleus or cytoplasm) nuc modified. Score: 0.90 Nuclear Signal Status: positive ( 0.70) Checking CaaX motif.. Checking N-myristoylation.. Checking CaaX motif.. Final Results nucleus Certainty= 0.880 (Affirmative) < suco mitochondrial matrix space Certainty= 0.360 (Affirmative) < suco lysosome (lumen) Certainty= 0.231 (Affirmative) < suco microbody (peroxisome) Certainty= 0.149 (Affirmative) < suco One predicted O-glycosylation site of SEQ ID NO: 6044 is identified at residue 4: Residue No. Potential Threshold Assignment Thr 4 0.6839 0.6484 T Accordingly, the invention comprises a polypeptide comprising a fragment of the amino acid sequence of SEQ JD NO: 6044, wherein said fragment comprises the O-glycosylation site identified above. The invention further comprises a polynucleotide encoding one or more of the polypeptides identified above. The invention includes a polypeptide comprising a fragment of SEQ ID NO: 6044 wherein said fragment does not include one or more of the glycosylation sites identified above. The invention also includes a polynucleotide encoding such a polypeptide. T-epitopes for SEQ ID NO: 6044 are identified in Table 18. The invention includes a polypeptide for use as an antigen, wherein the polypeptide comprises: (a) an amino acid sequence selected from the group consisting of the T-epitope sequences identified in SEQ ID NOS: 8487-8665; (b) an amino acid sequence having sequence identity to an amino acid sequence of (a). The invention further comprising a polynucleotide sequence encoding the polypeptides of (a) or (b). The invention further comprising a method of expression or delivery of such polynucleotides through viral vectors and/or viral particles. The invention further comprises a polypeptide comprising two or more of the T-epitope sequences identified in SEQ ID NOS: 8487-8665, or a polynucleotide encoding such a polypeptide. The use as an antigen is preferably a use: (1) as a T-cell antigen; (2) for generating a complex between a class I MHC protein (e.g. a class I HLA) and a fragment of said antigen; (3) as an antigen for raising a cell-mediated immune response; and/or (4) as an antigen for raising a CTL response. The use preferably protects or treats disease and/or infection caused by a SARS virus. The invention provides the use of a polypeptide in the manufacture of a medicament for immunising a mammal (typically a human) against SARS viral infection wherein the polypeptide is as defined above. The invention provides a method of raising an immune response in a mammal (typically a human), comprising the step of administering to the mammal a polypeptide as defined above, wherein said immune response is a cell-mediated immune response and, preferably, a CTL response. The immune response is preferably protective or therapeutic. The invention includes a polypeptide sequence comprising SEQ JD NO: 6045. The invention includes a polypeptide sequence comprising an amino acid sequence having sequence identity to SEQ ID NO: 6045. The invention includes a polypeptide sequence comprising a fragment of SEQ ID NO: 6045. The invention includes a polynucleotide sequence encoding any of these polypeptides. SEQ JD NO: 6045 demonstrates functional homology with the envelope or small membrane protein of coronaviruses. The invention includes a diagnostic kit comprising a polypeptide comprising SEQ JD NO: 6045 or a fragment thereof. The invention includes a diagnostic kit comprising a polynucleotide encoding SEQ JD NO: 6045 or a fragment thereof. The invention includes an immunogenic composition comprising SEQ JD NO: 6045 or a fragment thereof. The invention includes an antibody which recognizes a polypeptide comprising SEQ JD NO: 6045 or a fragment thereof. Predicted transmembrane regions of SEQ ID NO: 6045 are identified below: Inside to outside helices : 1 found from to score center 17 ( 19 ) 33 ( 33 ) 2881 26 Outside to inside helices : 1 found from to score center 17 ( 17 ) 34 ( 34 ) 2981 27 Accordingly, the invention includes a polypeptide comprising a fragment of SEQ ID NO: 6045 wherein said fragment does not include one or more of the hydrophobic amino acid sequences identified above. Preferably, the fragment does not include the amino acids between positions 17 to 34. The invention also includes a polynucleotide sequence encoding any of the above-identified polypeptides. In one embodiment, the invention includes a polypeptide comprising a fragment of SEQ ID NO: 6045 wherein said fragment does not include amino acid residues 1-34 of SEQ ID NO: 6045. Predicted protein Localization Site of SEQ JD NO: 6045 is below. PSORT Prediction of Protein Localization Sites for SEQ ID NO : 6045 version 6 .4 (WWW) Species classification : 4 *** Reasoning Step: 1 Preliminary Calculation of ALOM (threshold: 0.5) count : 2 Position of the most N-terminal TMS: 17 at i=l 5 MTOP: membrane topology (Hartmann et al . ) I (middle): 24 Charge diffirence(C-N) : 2.0 McG: Examining signal sequence (McGeoch) Length of UR: 29 Peak Value of UR: 3.40 0 Net Charge of CR: -2 Discriminant Score: 13.07 GvH: Examining signal sequence (von Heijne) Signal Score (-3.5): 4.37 Possible cleavage site: 32 5 ... positive value of mtop ... >» Seems to have an uncleavable N-term signal seq. Amino Acid Composition of Predicted Mature Form: calculated from 1 ALOM new cnt: 1 ** thrshld changed to -2 0 Cleavable signal was detected in ALOM? : 0B ALOM: finding transmembrane regions (Klein et al . ) count: 1 value: -15.12 threshold: -2.0 INTEGRAL Likelihood =-15.12 Transmembrane 17 - 33 ( 8 - 44) PERIPHERAL Likelihood = 0.47 5 modified ALOM score: 3.12 >» Seems to be a Type lb (Nexo Ccyt) membrane protein The cytoplasmic tail is from 34 to 76 (44 Residues) Rule: vesicular pathway Rule: vesicular pathway 0 Rule: vesicular pathway ( 6) or uncleavable? Gavel: Examining the boundary of mitochondrial targeting seq. motif at: 6 Uncleavable? Ipos set to: 16 5 Discrimination of mitochondrial target seq. : notclr ( 0.19) Rule: vesicular pathway Rule: vesicular pathway Rule: vesicular pathway 10 *** Reasoning Step: 2 > Relative position of the end of the tail: 44% Memb.protein with uncleavable signl is often at ER 1-5 KDEL Count: 0 Checking apolar signal for intramitochondrial sorting (Gavel position 16) from: 70 to: 99 Score: 21.5 >» Seems to have an intramitochondrial signal SKL motif (signal for peroxisomal protein) : !0 pos: -1(76), count: 0 Amino Acid Composition Tendency for Peroxisome: -4.11 Peroxisomal proteins? Status: negative Amino Acid Composition tendency for lysosomal proteins score: 0.68 Status: notclr 5 Checking the amount of Basic Residues (nucleus) Checking the 4 residue pattern for Nuclear Targeting Checking the 7 residue pattern for Nuclear Targeting Checking the Robbins & Dingwall consensus (nucleus) Checking the RNA binding motif (nucleus or cytoplasm) 0 Nuclear Signal Status: negative ( 0.00) Check cytoplasmic tail for typelb (plasma memb.) Checking the NPXY motif.. Checking the YXRF motif .. Checking N-myristoylation.. Final Results plasma membrane Certainty^ 0.730 (Affirmative) < suco endoplasmic reticulum (membrane) Certainty= 0.640 (Affirmative) < suco endoplasmic reticulum (lumen) Certainty= 0.100 (Affirmative) < suco outside Certainty= 0.100 (Affirmative) < suco Predicted N-glycosylation sites of SEQ ID NO: 6045 are identified at residues 48 and 66: Position Potential Jury NGlyc agreement result 48 NVSL 0.6514 (9/9) ++ (SEQ ID NO: 7266) 66 NSSE 0.5880 (7/9) + (SEQ ID NO: 7267) Accordingly, the invention comprises a polypeptide comprising a fragment of the amino acid sequence of SEQ ID NO: 6045, wherein said fragment comprises one or more of the N-glycosylation sites identified above. The invention comprises a polypeptide comprising a fragment of SEQ JD NO: 6045 wherein said fragment comprises one or more of the N- glycosylation sites identified above. The invention further comprises a polynucleotide encoding one or more of the polypeptides identified above. The invention includes a polypeptide comprising a fragment of SEQ ID NO: 6045 wherein said fragment does not include one or more of the glycosylation sites identified above. The invention also includes a polynucleotide encoding such a polypeptide. T-epitopes for SEQ ID NO: 6045 are identified in Table 19. The invention includes a polypeptide for use as an antigen, wherein the polypeptide comprises: (a) an amino acid sequence selected from the group consisting of the T-epitope sequences identified in SEQ JD NOS: 8666-8820; (b) an amino acid sequence having sequence identity to an amino acid sequence of (a). The invention further comprising a polynucleotide sequence encoding the polypeptides of (a) or (b). The invention further comprising a method of expression or delivery of such polynucleotides through viral vectors and/or viral particles. The invention further comprises a polypeptide comprising two or more of the T-epitope sequences identified in SEQ ID NOS: 8666-8820, or a polynucleotide encoding such a polypeptide. The use as an antigen is preferably a use: (1) as a T-cell antigen; (2) for generating a complex between a class I MHC protein (e.g. a class I HLA) and a fragment of said antigen; (3) as an antigen for raising a cell-mediated immune response; and/or (4) as an antigen for raising a CTL response. The use preferably protects or treats disease and or infection caused by a SARS virus. The invention provides the use of a polypeptide in the manufacture of a medicament for immunising a mammal (typically a human) against SARS viral infection wherein the polypeptide is as defined above. The invention provides a method of raising an immune response in a mammal (typically a human), comprising the step of administering to the mammal a polypeptide as defined above, wherein said immune response is a cell-mediated immune response and, preferably, a CTL response. The immune response is preferably protective or therapeutic. The invention includes a polypeptide sequence comprising SEQ JD NO: 6046. The invention includes polypeptide sequences comprising an amino acid sequence having sequence identity to SEQ JD NO: 6046. The invention includes a polypeptide sequence comprising a fragment of SEQ ID NO: 6046. The invention includes a polynucleotide encoding one of these polypeptides. SEQ ID NO: 6046 has functional homology with a matrix protein of a coronavirus. The invention includes a diagnostic kit comprising a polypeptide comprising SEQ ID NO: 6046 or a fragment thereof. The invention includes a diagnostic kit comprising a polynucleotide encoding SEQ JD NO: 6046 or a fragment thereof. The invention includes an immunogenic composition comprising SEQ ID NO: 6046 or a fragment thereof. The invention includes an antibody which recognizes a polypeptide comprising SEQ ID NO: 6046 or a fragment thereof. Predicted transmembrane regions of SEQ ID NO: 6046 are identified below. Inside to outside helices : 3 found from to score center 21 ( 21 ) 38 ( 36 ) 2412 29 51 ( 53 ) 69 ( 69 ) 2645 60 74 ( 82 ) 96 ( 96 ) 2464 89 Outside to inside helices : 3 found from to score center 18 ( 21 ) 38 ( 38 ) 2363 28 52 ( 52 ) 67 ( 67 ) 2363 60 76 ( 76 ) 95 ( 92 ) 2605 84 Accordingly, the invention includes a polypeptide comprising a fragment of SEQ ID NO: 6046 wherein said fragment does not include one or more of the hydrophobic amino acid sequences identified above. Preferably, the fragment does not include the amino acids between positions selected from the group consisting of 18 to 38, 52 to 67 and 76 to 95. The invention also includes a polynucleotide sequence encoding any of the above-identified polypeptides. Predicted protein localization of SEQ JD NO: 6046 is set forth below. PSORT Prediction of Protein Localization Sites version 6 .4 (WWW) Species classification: 4 *** Reasoning Step: 1 Preliminary Calculation of ALOM (threshold: 0.5) count : 3 Position of the most N-terminal TMS: 21 at i=l MTOP: membrane topology (Hartmann et al . ) I (middle): 28 Charge diffirence (C-N) : 6.0 McG: Examining signal sequence (McGeoch) Length of UR: 1 Peak Value of UR: 3.16 Net Charge of CR: -3 Discriminant Score: 2.21 GvH: Examining signal sequence (von Heijne) Signal Score (-3.5): 4.29 Possible cleavage site: 39 ... positive value of mtop ... >» Seems to have an uncleavable N-term signal seq. Amino Acid Composition of Predicted Mature Form: calculated from 1 Cleavable signal was detected in ALOM? : 0B ALOM: finding transmembrane regions (Klein et al . ) count: 3 value: -7.64 threshold: 0.5 INTEGRAL Likelihood -7. .64 Transmembrane 21 - 37 ( 18 - 39) INTEGRAL Likelihood -7. .59 Transmembrane 50 - 66 ( 43 - 72) INTEGRAL Likelihood -5. .04 Transmembrane 79 - 95 ( 72 - 99) PERIPHERAL Likelihood 2. .38 modified ALOM score: 13 >» Likely a Type Illb membrane protein (Nexo Ccyt) Rule: vesicular pathway Rule: vesicular pathway Rule: vesicular pathway ( 2) or uncleavable? Gavel: Examining the boundary of mitochondrial targeting seq. motif at: 2 Uncleavable? Ipos set to : 12 Discrimination of mitochondrial target seq. : negative (-4.16) Rule: vesicular pathway Rule: vesicular pathway Rule: vesicular pathway *** Reasoning Step: 2 Type Ilia or Illb is favored for ER memb. proteins Memb.protein with uncleavable signl is often at ER KDEL Count : 0 Checking apolar signal for intramitochondrial sorting SKL motif (signal for peroxisomal protein) : pos: -1(221), count: 0 Amino Acid Composition Tendency for Peroxisome: 5.01 Peroxisomal proteins? Status: notclr Amino Acid Composition tendency for lysosomal proteins score: 2.30 Status: positive Type III proteins may be localized at Golgi Checking the amount of Basic Residues (nucleus) Checking the 4 residue pattern for Nuclear Targeting Checking the 7 residue pattern for Nuclear Targeting Checking the Robbins & Dingwall consensus (nucleus) Checking the RNA binding motif (nucleus or cytoplasm) Nuclear Signal Status: negative ( 0.00) Check the Number of TMSs for typelll (plasma memb.) Checking N-myristoylation.. Final Results endoplasmic reticulum (membrane) Certainty= 0.685 (Affirmative) < suco plasma membrane Certainty= 0.640 (Affirmative) < suco Golgi body Certainty= 0.460 (Affirmative) < suco endoplasmic reticulum (lumen) Certainty= 0.100 (Affirmative) < suco One predicted N-glycosylation sites of SEQ ID NO: 6046 is identified at residue 4: Prediction ofN-slvcosylation sites Position Potential Jury NGlyc agreement result 4 NGTI 0.8430 (9/9) +++ (SEQ ID NO: 7268) Accordingly, the invention comprises a polypeptide comprising a fragment of the amino acid sequence of SEQ JD NO: 6046, wherein said fragment comprises the N-glycosylation site identified above. The invention further comprises a polynucleotide encoding one or more of the polypeptides identified above. The invention further comprises a polypeptide comprising a fragment of amino acid sequence SEQ ID NO: 6046, wherein said fragment does not include the N-glycosylation site identified above. The invention includes a polynucleotide encoding such a fragment. A variant of SEQ JD NO: 6046 that is included within the invention is SEQ ID NO: 9963. Compared to SEQ ID NO: 6046, this sequence has Val at residue 72 instead of Ala. T-epitopes for SEQ ID NO: 6046 are identified in Table 20. The invention includes a polypeptide for use as an antigen, wherein the polypeptide comprises: (a) an amino acid sequence selected from the group consisting of the T-epitope sequences identified in SEQ JD NOS: 8821-9018; (b) an amino acid sequence having sequence identity to an amino acid sequence of (a). The invention further comprising a polynucleotide sequence encoding the polypeptides of (a) or (b). The invention further comprising a method of expression or delivery of such polynucleotides through viral vectors and/or viral particles. The invention further comprises a polypeptide comprising two or more of the T-epitope sequences identified in SEQ JD NOS: 8821-9018, or a polynucleotide encoding such a polypeptide. The use as an antigen is preferably a use: (1) as a T-cell antigen; (2) for generating a complex between a class I MHC protein (e.g. a class I HLA) and a fragment of said antigen; (3) as an antigen for raising a cell-mediated immune response; and/or (4) as an antigen for raising a CTL response. The use preferably protects or treats disease and/or infection caused by a SARS virus. The invention provides the use of a polypeptide in the manufacture of a medicament for immunising a mammal (typically a human) against SARS viral infection wherein the polypeptide is as defined above. The invention provides a method of raising an immune response in a mammal (typically a human), comprising the step of administering to the mammal a polypeptide as defined above, wherein said immune response is a cell-mediated immune response and, preferably, a CTL response. The immune response is preferably protective or therapeutic. The invention includes a polypeptide sequence comprising SEQ JD NO: 6047 or a fragment thereof or an amino acid sequence having sequence identity thereto. Predicted transmembrane regions of SEQ ID NO: 6047 are identified below. Inside to outside helices : 2 found from to score center 7 ( 10 ) 29 ( 27 ) 729 17 21 ( 24 ) 41 ( 41 ) 640 34 Outside to inside helices : 2 found from to score center 4 ( 4) 22 ( 19) 874 12 22 ( 24) 41 ( 41) 499 31 Accordingly, the invention includes a polypeptide comprising a fragment of SEQ JD NO: 6047 wherein said fragment does not include one or more of the hydrophobic amino acid sequences identified above. Preferably, the fragment does not include the amino acids between positions selected from the group consisting of 4 to 22 and 22 to 41. The invention also includes a polynucleotide sequence encoding any of the above-identified polypeptides. SEQ ID NO: 6047 is predicted to be a hypothetical protein of SARS virus. A prediction of the protein localization of SEQ JD NO: 6047 is set forth below. SEQ ID NO: 6047 is predicted to be located in one of the following locations: plasma membrane, endoplasmic reticulum, Golgi body, and microbody (peroxisome). SEQ ID NO: 6047 may be associated with an organelle inside an infected cell or with viral entry to a host cell. Accordingly, SEQ LD NO: 6047 is a target for screening of chemical inhibitors to the SARS virus. The invention includes a polypeptide comprises SEQ JD NO: 6047 or a fragment thereof. The invention includes a polynucleotide encoding the polypeptide sequence of SEQ JD NO: 6047 or a fragment thereof. The invention includes a method of screening SEQ ID NO: 6047 for an inhibitor. The invention includes the recombinant expression of SEQ ID NO: 6047 in a host cell. The invention includes a small molecule which prevents the polypeptide of SEQ ID NO: 6047 from associating with an organelle inside of an infected cell or interacting with a host cell membrane. The invention includes a fusion protein wherein said fusion protein comprises SEQ ID NO: 6047. Predicted protein localization of SEQ JD NO: 6047 is set forth below. PSORT Prediction of Protein Localization Sites version 6.4 (WWW) Species classification: 4 *** Reasoning Step: 1 Preliminary Calculation of ALOM (threshold: 0.5) count : 1 Position of the most N-terminal TMS: 2 at i=l MTOP: membrane topology (Hartmann et al . ) I (middle): 9 Charge diffirence(C-N) : 0.5 McG: Examining signal sequence (McGeoch) Length of UR: 6 Peak Value of UR: 3.08 Net Charge of CR: 0 Discriminant Score: 5.12 GvH: Examining signal sequence (von Heijne) Signal Score (-3.5): -4.45 Possible cleavage site: 34 »> Seems to have an uncleavable N-term signal seq. Amino Acid Composition of Predicted Mature Form: calculated from 1 ALOM new cnt: 1 ** thrshld changed to -2 Cleavable signal was detected in ALOM?: 0B ALOM: finding transmembrane regions (Klein et al . ) count: 1 value: -2.44 threshold: -2.0 INTEGRAL Likelihood = -2.44 Transmembrane 2 - 18 ( 1 - 20) PERIPHERAL Likelihood = 1.22 modified ALOM score: 0.59 >» Seems to be a Type II (Ncyt Cexo) membrane protein The cytoplasmic tail is from 1 to 1 (1 Residues) Rule: vesicular pathway Rule: vesicular pathway Rule: vesicular pathway ( 5) or uncleavable? Gavel: Examining the boundary of mitochondrial targeting seq. motif at: 5 Uncleavable? Ipos set to: 15 Discrimination of mitochondrial target seq. : notclr ( 1.48) Rule: vesicular pathway Rule: vesicular pathway Rule: vesicular pathway *** Reasoning Step: 2 Relative position of the cytoplasmic tail: 1% Larger value (>30%) is favared for ER memb. proteins Memb.protein with uncleavable signl is often at ER KDΞL Count: 0 Checking apolar signal for intramitochondrial sorting (Gavel position 15) from: 64 to: 93 Score: 30.0 >» Seems to have an intramitochondrial signal SKL motif (signal for peroxisomal protein) : pos: -1(63), count: 0 Amino Acid Composition Tendency for Peroxisome: 1.91 Peroxisomal proteins? Status: notclr AAC score (peroxisome): 0.161 Amino Acid Composition tendency for lysosomal proteins score: 0.04 Status: notclr Checking the consensus for Golgi Checking the consensus for Golgi Checking the cytoplasmic tail of type II. (Golgi) Checking the amount of Basic Residues (nucleus) Checking the 4 residue pattern for Nuclear Targeting Checking the 7 residue pattern for Nuclear Targeting Checking the Robbins & Dingwall consensus (nucleus) Checking the RNA binding motif (nucleus or cytoplasm) Nuclear Signal Status: negative ( 0.00) Check mitochondrial signal for typell (plasma memb.) Type II is favored for plasma memb. proteins Checking the NPXY motif.. Checking the YXRF motif... Checking N-myristoylation.. Final Results plasma membrane Certainty= 0.685 (Affirmative) < suco endoplasmic reticulum (membrane) Certainty= 0.640 (Affirmative) < suco Golgi body Certainty= 0.370 (Affirmative) < suco microbody (peroxisome) Certainty= 0.161 (Affirmative) < suco T-epitopes for SEQ ID NO: 6047 are identified in Table 21. The invention includes a polypeptide for use as an antigen, wherein the polypeptide comprises: (a) an amino acid sequence selected from the group consisting of the T-epitope sequences identified in SEQ JD NOS: 9019-9131; (b) an amino acid sequence having sequence identity to an amino acid sequence of (a). The invention further comprising a polynucleotide sequence encoding the polypeptides of (a) or (b). The invention further comprising a method of expression or delivery of such polynucleotides through viral vectors and/or viral particles. The invention further comprises a polypeptide comprising two or more of the T-epitope sequences identified in SEQ JD NOS: 9019-9131, or a polynucleotide encoding such a polypeptide. The use as an antigen is preferably a use: (1) as a T-cell antigen; (2) for generating a complex between a class I MHC protein (e.g. a class I HLA) and a fragment of said antigen; (3) as an antigen for raising a cell-mediated immune response; and/or (4) as an antigen for raising a CTL response. The use preferably protects or treats disease and/or infection caused by a SARS virus. The invention provides the use of a polypeptide in the manufacture of a medicament for immunising a mammal (typically a human) against SARS viral infection wherein the polypeptide is as defined above. The invention provides a method of raising an immune response in a mammal (typically a human), comprising the step of administering to the mammal a polypeptide as defined above, wherein said immune response is a cell-mediated immune response and, preferably, a CTL response. The immune response is preferably protective or therapeutic. The invention includes a polypeptide comprising SEQ JD NO: 6048, a fragment thereof or an amino acid sequence having sequence identity thereto. Predicted transmembrane regions of SEQ ID NO: 6048 are identified below. Inside to outside helices : 2 found from to score center 3 ( 3) 18 ( 18) 1857 10 100 ( 100) 117 ( 115) 2904 107 Outside to inside helices : 2 found from to score center 1 ( 1) 15 ( 15) 1299 8 100 ( 100) 117 ( 115) 3009 107 Accordingly, the invention includes a polypeptide comprising a fragment of SEQ JD NO: 6048 wherein said fragment does not include one or more of the hydrophobic amino acid sequences identified above. Preferably, the fragment does not include the amino acids between positions selected from the group consisting of 1 to 15 and 100 to 117. The invention also includes a polynucleotide sequence encoding any of the above-identified polypeptides. SEQ JD NO: 6048 is predicted to be a hypothetical protein of SARS virus. A prediction of 5 the protein localization of SEQ JD NO: 6048 is set forth below. SEQ ID NO: 6048 is predicted to be located in one of the following locations: plasma membrane, lysosome (membrane), microbody (peroxisome), and endoplasmic reticulum (membrane). SEQ ID NO: 6048 may be associated with an organelle inside an infected cell or may interact with a host cell plasma membrane during viral entry to the host cell. 0 Accordingly, SEQ ID NO: 6048 is a target for screening of chemical inhibitors to the SARS virus. The invention includes a polypeptide comprises SEQ ID NO: 6048 or a fragment thereof. The invention includes a polynucleotide encoding the polypeptide sequence of SEQ ID NO: 6048 or a fragment thereof. The invention includes a method of screening SEQ ID NO: 6048 for an inhibitor. The invention includes the recombinant expression of SEQ JD NO: 6048 5 in a host cell. The invention includes a small molecule which prevents the polypeptide of SEQ ID NO: 6048 from associating with an organelle inside of an infected cell or prevents the polypeptide from associating with the cell membrane of a host cell. The invention includes a fusion protein wherein said fusion protein comprises SEQ ID NO: 6048. Predicted protein localization of SEQ JD NO: 6048 is set forth below. 10 PSORT Prediction of Protein Localization Sites version 6.4 (WWW) Species classification: 4 *** Reasoning Step: 1 :5 Preliminary Calculation of ALOM (threshold: 0.5) count : 2 Position of the most N-terminal TMS: 3 at i=2 MTOP: membrane topology (Hartmann et al . ) 0 I (middle): 10 Charge diffirence(C-N) : -2.5 McG: Examining signal sequence (McGeoch) Length of UR: 13 Peak Value of UR: 3.38 Net Charge of CR: 1 5 Discriminant Score: 10.02 GvH: Examining signal sequence (von Heijne) Signal Score (-3.5): 2.56 Possible cleavage site: 15 >» Seems to have a cleavable N-term signal seq. 3 Amino Acid Composition of Predicted Mature Form: calculated from 16 ALOM new cnt: 2 ** thrshld changed to -2 Cleavable signal was detected in ALOM? : IB ALOM: finding transmembrane regions (Klein et al . ) 5 count: 1 value: -14.75 threshold: -2.0 INTEGRAL Likelihood =-14.75 Transmembrane 101 - 117 ( 95 - 120) PERIPHERAL Likelihood = 6.63 modified ALOM score: 3.05 »> Seems to be a Type la membrane protein The cytoplasmic tail is from 118 to 122 (5 Residues) Rule: vesicular pathway Rule: vesicular pathway Rule: vesicular pathway (15) or uncleavable? Gavel: Examining the boundary of mitochondrial targeting seq. motif at: 15 Uncleavable? Ipos set to: 25 Discrimination of mitochondrial target seq. : notclr ( 0.73) Rule: vesicular pathway Rule: vesicular pathway Rule: vesicular pathway *** Reasoning Step: 2 KDEL Count : 0 Checking apolar signal for intramitochondrial sorting (Gavel position 25) from: 3 to: 12 Score: 8.5 SKL motif (signal for peroxisomal protein) : pos: -1(122), count: 0 Amino Acid Composition Tendency for Peroxisome: 2.46 AAC not from the N-term. , score modified Peroxisomal proteins? Status: notclr AAC score (peroxisome): 0.115 Amino Acid Composition tendency for lysosomal proteins score: -0.40 Status: negative GY motif in the tail of typela? (lysosomal) Checking the amount of Basic Residues (nucleus) Checking the 4 residue pattern for Nuclear Targeting Checking the 7 residue pattern for Nuclear Targeting Checking the Robbins & Dingwall consensus (nucleus) Checking the RNA binding motif (nucleus or cytoplasm) Nuclear Signal Status: negative ( 0.00) Type la is favored for plasma memb. proteins Checking the NPXY motif .. Checking the YXRF motif.. Checking N-myristoylation.. Checking GPI anchor .. >» Seems to be GPI-anchored (0.85) Final Results plasma membrane Certainty= 0.919 (Affirmative) < suco lysosome (membrane) Certainty= 0.200 (Affirmative) < suco microbody (peroxisome) Certainty= 0.115 (Affirmative) < suco endoplasmic reticulum (membrane) Certainty= 0.100 (Affirmative) < suco T-epitopes for SEQ JD NO: 6048 are identified in Table 22. The invention includes a polypeptide for use as an antigen, wherein the polypeptide comprises: (a) an amino acid sequence selected from the group consisting of the T-epitope sequences identified in SEQ ID NOS: 9132-9308; (b) an amino acid sequence having sequence identity to an amino acid sequence of (a). The invention further comprising a polynucleotide sequence encoding the polypeptides of (a) or (b). The invention further comprising a method of expression or delivery of such polynucleotides through viral vectors and/or viral particles. The invention further comprises a polypeptide comprising two or more of the T-epitope sequences identified in SEQ ID NOS: 9132-9308, or a polynucleotide encoding such a polypeptide. The use as an antigen is preferably a use: (1) as a T-cell antigen; (2) for generating a complex between a class I MHC protein (e.g. a class I HLA) and a fragment of said antigen; (3) as an antigen for raising a cell-mediated immune response; and/or (4) as an antigen for raising a CTL response. The use preferably protects or treats disease and/or infection caused by a SARS virus. The invention provides the use of a polypeptide in the manufacture of a medicament for immunising a mammal (typically a human) against SARS viral infection wherein the polypeptide is as defined above. The invention provides a method of raising an immune response in a mammal (typically a human), comprising the step of administering to the mammal a polypeptide as defined above, wherein said immune response is a cell-mediated immune response and, preferably, a CTL response. The immune response is preferably protective or therapeutic. The invention includes a polypeptide comprising SEQ JD NO: 6049, a fragment thereof or an amino acid sequence having sequence identity thereto. Predicted transmembrane or hydrophobic regions of SEQ JD NO: 6049 are identified below. Inside to outside helices : 1 found from to score center 13 ( 13 ) 30 ( 28 ) 3532 20 Outside to inside helices : 1 found from to score center 9 ( 11) 29 ( 26) 3395 19 Accordingly, the invention includes a polypeptide comprising a fragment of SEQ JD NO: 6049 wherein said fragment does not include one or more of the hydrophobic amino acid sequences identified above. The invention also includes a polynucleotide sequence encoding any of the above-identified polypeptides. SEQ JD NO: 6049 is predicted to be a hypothetical protein of SARS virus. A prediction of the protein localization of SEQ ID NO: 6049 is set forth below. SEQ JD NO: 6049 is predicted to be located in one of the following locations: outside, microbody (peroxisome), endoplasmic reticulum (membrane) and endoplasmic reticulum (lumen). The highest ranking indicates that SEQ ID NO: 6049 is located on the outside of a cell. Accordingly, SEQ ID NO: 6049 may be a surface exposed protein. Accordingly, SEQ JD NO: 6049 may be used in an immunogenic composition to raise an immune response against the SARS virus. It also may be used to generate antibodies specific to the SARS virus. Such antibodies may be used in a method of treatment or prevention of a SARS virus infection. Such antibodies may further be used in a diagnostic test to identify the presence or absence of SARS virus in a biological sample. The invention includes a polypeptide comprises SEQ ID NO: 6049 or a fragment thereof. The invention includes a polynucleotide encoding the polypeptide sequence of SEQ ID NO: 6049 or a fragment thereof. The invention includes a method of screening SEQ JD NO: 6049 for an inhibitor. The invention includes the recombinant expression of SEQ ID NO: 6049 in a host cell. The invention includes a fusion protein wherein said fusion protein comprises SEQ ID NO: 6049. Predicted protein localization of SEQ ID NO: 6049 is set forth below. PSORT Prediction of Protein Localization Sites version 6.4 (WWW) Species classification: 4 0 *** Reasoning Step: 1 Preliminary Calculation of ALOM (threshold: 0.5) count : 1 5 Position of the most N-terminal TMS: 11 at i=l MTOP: membrane topology (Hartmann et al . ) I (middle): 18 Charge diffirence (C-N) : -2.0 McG: Examining signal sequence (McGeoch) Length of UR: 24 0 Peak Value of UR: 3.69 Net Charge of CR: -2 Discriminant Score: 13.56 GvH: Examining signal sequence (von Heijne) Signal Score (-3.5): 0.52 5 Possible cleavage site: 25 >» Seems to have a cleavable N-term signal seq. Amino Acid Composition of Predicted Mature Form: calculated from 26 ALOM new cnt : 1 ** thrshld changed to -2 0 Cleavable signal was detected in ALOM? : IB ALOM: finding transmembrane regions (Klein et al . ) count: 0 value: 14.80 threshold: -2.0 PERIPHERAL Likelihood = 14.80 modified ALOM score: -3.86 5 Rule: vesicular pathway Rule: vesicular pathway Rule: vesicular pathway ( 2) or uncleavable? Gavel: Examining the boundary of mitochondrial targeting seq. 1-0 motif at: 2 Uncleavable? Ipos set to: 12 Discrimination of mitochondrial target seq. : notclr ( 1.42) Rule: vesicular pathway ■ 5 Rule: vesicular pathway Rule: vesicular pathway *** Reasoning Step: 2 0 KDEL Count: 0 Number of Potential N-glycosylation Sites : 0 Out: score 0.800 Checking apolar signal for intramitochondrial sorting (Gavel position 12) from: 44 to: 73 Score: 30.0 5 »> Seems to have an intramitochondrial signal SKL motif (signal for peroxisomal protein) : pos: -1(44), count: 0 Amino Acid Composition Tendency for Peroxisome : 9 . 47 AAC not from the N-term. , score modified Peroxisomal proteins? Status : notclr AAC score (peroxisome) : 0 . 320 Amino Acid Composition tendency for lysosomal proteins score : -6 . 47 Status : negative Number of NX ( S/T) motif : 0 Checking the amount of Basic Residues (nucleus ) Checking the 4 residue pattern for Nuclear Targeting Checking the 7 residue pattern for Nuclear Targeting Checking the Robbins & Dingwall consensus (nucleus ) Checking the RNA binding motif (nucleus or cytoplasm) Nuclear Signal Status : negative ( 0 . 00 ) Checking CaaX motif . . Checking N-myristoylation . . Checking CaaX motif . . Final Results outside Certainty= 0.820 (Affirmative) < suco microbody (peroxisome) Certainty= 0 .320 (Affirmative) < suco endoplasmic reticulum (membrane) Certainty= 0 .100 (Affirmative) < suco endoplasmic reticulum (lumen) Certainty= 0 .100 (Affirmative) < suco T-epitopes for SEQ ID NO: 6049 are identified in Table 23. The invention includes a polypeptide for use as an antigen, wherein the polypeptide comprises: (a) an amino acid sequence selected from the group consisting of the T-epitope sequences identified in SEQ ID NOS: 9309-9437; (b) an amino acid sequence having sequence identity to an amino acid sequence of (a). The invention further comprising a polynucleotide sequence encoding the polypeptides of (a) or (b). The invention further comprising a method of expression or delivery of such polynucleotides through viral vectors and/or viral particles. The invention further comprises a polypeptide comprising two or more of the T-epitope sequences identified in SEQ JD NOS: 9309-9437, or a polynucleotide encoding such a polypeptide. The use as an antigen is preferably a use: (1) as a T-cell antigen; (2) for generating a complex between a class I MHC protein (e.g. a class I HLA) and a fragment of said antigen; (3) as an antigen for raising a cell-mediated immune response; and/or (4) as an antigen for raising a CTL response. The use preferably protects or treats disease and/or infection caused by a SARS virus. The invention provides the use of a polypeptide in the manufacture of a medicament for immunising a mammal (typically a human) against SARS viral infection wherein the polypeptide is as defined above. The invention provides a method of raising an immune response in a mammal (typically a human), comprising the step of administering to the mammal a polypeptide as defined above, wherein said immune response is a cell-mediated immune response and, preferably, a CTL response. The immune response is preferably protective or therapeutic. The invention includes a polypeptide comprising SEQ JD NO: 6050 or a fragment thereof or an amino acid sequence having sequence identity thereto. Predicted transmembrane or hydrophobic regions are identified below. Inside to outside helices : 1 found 5 from to score center 13 ( 15 ) 32 ( 30 ) 558 23 Outside to inside helices : 1 found from to score center 0 16 ( 16 ) 30 ( 30 ) 364 23 Accordingly, the invention includes a polypeptide comprising a fragment of SEQ JD NO: 6050 wherein said fragment does not include one or more of the hydrophobic amino acid sequences identified above. The invention also includes a polynucleotide sequence encoding any 5 of the above-identified polypeptides . SEQ ID NO: 6050 is predicted to be a hypothetical protein of SARS virus. A prediction of the protein localization of SEQ ID NO: 6050 is set forth below. SEQ ID NO: 6050 is predicted to be located in one of the following locations: lysosome (lumen), mitochondrial matrix space, mitochondrial inner membrane, and mitochondrial intermembrane space. SEQ JD NO: 6050 0 may be associated with an organelle inside an infected cell during the viral replication cycle. Accordingly, SEQ ID NO: 6050 is a target for screening of chemical inhibitors to the SARS virus. The invention includes a polypeptide comprises SEQ JD NO: 6050 or a fragment thereof. The invention includes a polynucleotide encoding the polypeptide sequence of SEQ JD NO: 6050 or a fragment thereof. The invention includes a method of screening SEQ ID NO: 25 6050 for an inhibitor. The invention includes the recombinant expression of SEQ JD NO: 6050 in a host cell. The invention includes a small molecule which prevents the polypeptide of SEQ JD NO: 6050 from associating with an organelle inside of an infected cell or prevents the polypeptide from associating with the cell membrane of a host cell. The invention includes a fusion protein wherein said fusion protein comprises SEQ JD NO: 6050. Predicted protein !0 localization of SEQ JD NO: 6050 is set forth below. PSORT Prediction of Protein Localization Sites version 6.4 (WWW) MYSEQ 84 Residues Species classification: 4 15 *** Reasoning Step: 1 Preliminary Calculation of ALOM (threshold: 0.5) count : 0 ■ 0 McG: Examining signal sequence (McGeoch) Length of UR: 3 Peak Value of UR: 1.46 Net Charge of CR: 2 Discriminant Score: -5.73 5 GvH: Examining signal sequence (von Heijne) Signal Score (-3.5): -0.12 Possible cleavage site: 29 >» Seems to have no N-terminal signal seq. Amino Acid Composition of Predicted Mature Form: calculated from 1 ALOM new cnt: 0 ** thrshld changed to -2 Cleavable signal was detected in ALOM? : 0B ALOM: finding transmembrane regions (Klein et al . ) count: 0 value: 8.43 threshold: -2.0 PERIPHERAL Likelihood = 8.43 modified ALOM score: -2.59 Gavel: Examining the boundary of mitochondrial targeting seq. motif at: 61 ARCWYL Discrimination of mitochondrial target seq. : positive ( 1.66) Rule : mitochondrial protein Rule : mitochondrial protein Rule : mitochondrial protein Rule: mitochondrial protein *** Reasoning Step: 2 KDEL Count : 0 Checking apolar signal for intramitochondrial sorting (Gavel position 61) from: 52 to: 58 Score: 6.0 Mitochondrial matrix? Score: 0.38 SKL motif (signal for peroxisomal protein) : pos: -1(84), count: 0 Amino Acid Composition Tendency for Peroxisome: 1.47 Peroxisomal proteins? Status: notclr AAC score (peroxisome): 0.263 Amino Acid Composition tendency for lysosomal proteins score: 2.86 Status: positive Modified score for lysosome: 0.850 Checking the amount of Basic Residues (nucleus) Checking the 4 residue pattern for Nuclear Targeting Checking the 7 residue pattern for Nuclear Targeting Checking the Robbins & Dingwall consensus (nucleus) Checking the RNA binding motif (nucleus or cytoplasm) Nuclear Signal Status: negative ( 0.00) Checking CaaX motif.. Checking N-myristoylation.. Checking CaaX motif.. Final Results lysosome (lumen) Certainty= 0.850 (Affirmative) < suco mitochondrial matrix space Certainty= 0.54 (Affirmative) < suco mitochondrial inner membrane Certainty= 0.266 (Affirmative) < suco mitochondrial intermembrane space Certainty= 0.266 (Affirmative) < suco One predicted N-glycosylation sites of SEQ JD NO: 6050 is identified at residue 43: Position Potential Jury NGlyc agreement result 43 NVTI 0.6713 (9/9) ++ (SEQ ID NO: 7269) Accordingly, the invention comprises a polypeptide comprising a fragment of the amino acid sequence of SEQ JD NO: 6050 wherein said fragment comprises the N-glycosylation site identified above. The invention further comprises a polynucleotide encoding one or more of the polypeptides identified above. The invention further comprises a polypeptide comprising a fragment of amino acid sequence SEQ ID NO: 6050 wherein said fragment does not include the N-glycosylation site identified above. The invention includes a polynucleotide encoding such a fragment. T-epitopes for SEQ ID NO: 6050 are identified in Table 24. The invention includes a polypeptide for use as an antigen, wherein the polypeptide comprises: (a) an amino acid sequence selected from the group consisting of the T-epitope sequences identified in SEQ ID NOS: 9438-9538; (b) an amino acid sequence having sequence identity to an amino acid sequence of (a). The invention further comprising a polynucleotide sequence encoding the polypeptides of (a) or (b). The invention further comprising a method of expression or delivery of such polynucleotides through viral vectors and/or viral particles. The invention further comprises a polypeptide comprising two or more of the T-epitope sequences identified in SEQ JD NOS: 9438-9538, or a polynucleotide encoding such a polypeptide. The use as an antigen is preferably a use: (1) as a T-cell antigen; (2) for generating a complex between a class I MHC protein (e.g. a class I HLA) and a fragment of said antigen; (3) as an antigen for raising a cell-mediated immune response; and/or (4) as an antigen for raising a CTL response. The use preferably protects or treats disease and/or infection caused by a SARS virus. The invention provides the use of a polypeptide in the manufacture of a medicament for immunising a mammal (typically a human) against SARS viral infection wherein the polypeptide is as defined above. The invention provides a method of raising an immune response in a mammal (typically a human), comprising the step of administering to the mammal a polypeptide as defined above, wherein said immune response is a cell-mediated immune response and, preferably, a CTL response. The immune response is preferably protective or therapeutic. The invention includes a polypeptide sequence comprising SEQ ID NO: 6051 or a fragment thereof or an amino acid sequence having sequence identity thereto. The invention includes a polypeptide sequence comprising SEQ JD NO: 6052 or a fragment thereof or an amino acid sequence having sequence identity thereto. SEQ JD NO: 6051 and SEQ ID NO: 6052 demonstrate functional homology with a nucleocapsid protein of a coronavirus. The invention includes a diagnostic kit comprising a polypeptide comprising SEQ JD NO: 6051, SEQ JD NO: 6052 or a fragment thereof. The invention includes a diagnostic kit comprising a polynucleotide encoding SEQ ID NO: 6051, SEQ ID NO: 6052 or a fragment thereof. The invention includes an immunogenic composition comprising SEQ ID NO: 6051, SEQ ID NO: 6052 or a fragment thereof. The invention includes an antibody which recognizes a polypeptide comprising SEQ JD NO: 6051, SEQ ID NO: 6052 or a fragment thereof. SEQ JD NO: 6051 is predicted to be phosphorylated at Ser-79; Thr-92; Ser-106; Thr-116; Thr-142; Ser-184; Ser-188; Ser-202; Ser-236; Thr-248; Ser-251; Ser-256; Thr-377. Accordingly, the invention includes a polypeptide comprising a fragment of SEQ ID NO: 6051 wherein said fragment includes one or more of the amino acid residues of SEQ LD NO: 6051 selected from the group consisting of Ser-79; Thr-92; Ser-106; Thr-116; Thr-142; Ser-184; Ser- 188; Ser-202; Ser-236; Thr-248; Ser-251; Ser-256; Thr-377. The invention further includes a polypeptide comprising a fragment of SEQ JD NO: 6051 wherein said fragment does not include one or more of the amino acid residues of SEQ ID NO: 6051 selected from the group consisting of Ser-79; Thr-92; Ser-106; Thr-116; Thr-142; Ser-184; Ser-188; Ser-202; Ser-236; Thr-248; Ser-251; Ser-256; Thr-377. Two further useful fragments of the N protein (e.g. for immunoassay) are SEQ ID NOS: 9783 & 9784, which are lysine-rich and can be used to distinguish the SARS virus from other coronaviruses. Predicted transmembrane regions of SEQ JD NO: 6051 are identified below. Inside to outside helices : 1 found from to score center 304 ( 304) 323 ( 319 ) 495 312 Outside to inside helices : 2 found from to score center 304 ( 304) 319 ( 319 ) 597 312 Accordingly, the invention includes a polypeptide comprising a fragment of SEQ ID NO: 6051 wherein said fragment does not include one or more of the hydrophobic amino acid sequences identified above. The invention also includes a polynucleotide sequence encoding any of the above-identified polypeptides. Predicted protein localization of SEQ JD NO: 6051 is set forth below. SEQ ID NO: 6051 is predicted to be localized near the nucleus, lysosome (lumen), mitochondrial matrix space, and microbody (peroxisome). The highest ranking is for localization near the nucleus. Coronavirus nucleocapsid proteins are known to bind to viral RNA. Coronavirus nucleocapsid proteins are also thought to be important for cell mediated immunity. Accordingly, the invention includes a polynucleotide comprising SEQ JD NO: 6051. The invention further includes a viral vector or particle suitable for in vivo delivery of the polynucleotide sequence comprising a SARS virus nuceocapsid polynucleotide sequence or a fragment thereof. In one embodiment, the polynucleotide comprises SEQ ID NO: 6051 or a fragment thereof. The invention further includes a method for eliciting a cell mediated immune response comprising delivering a polynucleotide encoding a SARS virus nucleocapsid protein or a fragment thereof to a mammal. In one embodiment, the polynucleotide comprising SEQ ID NO: 6051 or a fragment thereof. The invention further includes a method of screening SEQ JD NO: 6051 for an inhibitor. The invention includes the recombinant expression of SEQ JD NO: 6051 in a host cell. The invention includes a small molecule which prevents the polypeptide of SEQ ID NO: 6051 from binding to SARS virus RNA during viral replication. The invention includes a fusion protein wherein said fusion protein comprises SEQ JD NO: 6051. Predicted protein localization of SEQ ID NO: 6051 is set forth below. PSORT Prediction of Protein Localization Sites version 6.4 (WWW) Species classification: 4 0 *** Reasoning Step: 1 Preliminary Calculation of ALOM (threshold: 0.5) count : 0 5 McG: Examining signal sequence (McGeoch) Length of UR: 3 Peak Value of UR: 0.19 Net Charge of CR: 0 Discriminant Score: -15.98 0 GvH: Examining signal sequence (von Heijne) Signal Score (-3.5): -6.36 Possible cleavage site: 58 >» Seems to have no N-terminal signal seq. Amino Acid Composition of Predicted Mature Form: 5 calculated from 1 ALOM new cnt: 0 ** thrshld changed to -2 Cleavable signal was detected in ALOM?: 0B ALOM: finding transmembrane regions (Klein et al . ) count: 0 value: 5.04 threshold: -2.0 0 PERIPHERAL Likelihood = 5.04 modified ALOM score: -1.91 Gavel: Examining the boundary of mitochondrial targeting seq. motif at: 17 PRITFG 5 Discrimination of mitochondrial target seq. : negative (-3.97) *** Reasoning Step: 2 10 KDEL Count: 0 Checking apolar signal for intramitochondrial sorting Mitochondrial matrix? Score: 0.10 SKL motif (signal for peroxisomal protein) : pos: -1(399), count: 0 15 Amino Acid Composition Tendency for Peroxisome: 0.04 Peroxisomal proteins? Status: notclr AAC score (peroxisome): 0.072 Amino Acid Composition tendency for lysosomal proteins score: 0.96 Status: notclr )0 Modified score for lysosome: 0.246 Checking the amount of Basic Residues (nucleus) Checking the 4 residue pattern for Nuclear Targeting Found: pos: 256 (4) KKPR Found: pos: 372 (5) KKKK !5 Checking the 7 residue pattern for Nuclear Targeting Checking the Robbins & Dingwall consensus (nucleus) Found: pos: 372 (3) KK KKTDEAQPLP QRQKK Found: pos: 373 (3) KK KTDEAQPLPQ RQKKQ Final Robbins Score (nucleus): 0.80 Checking the RNA binding motif (nucleus or cytoplasm) nuc modified. Score: 0.90 Nuclear Signal Status: positive ( 0.90) Checking CaaX motif.. Checking N-myristoylation.. Checking CaaX motif .. Final Results nucleus Certainty= 0.980 (Affirmative) < suco lysosome (lumen) Certainty= 0.246 (Affirmative) < suco mitochondrial matrix space Certainty= 0.100 (Affirmative) < suco microbody (peroxisome) Certainty= 0.072 (Affirmative) < suco Predicted N-glycosylation sites of SEQ JD NO: 6051 are identified below. Position Potential Jury NGlyc agreement result 48 NNTA 0.6879 (9/9) ++ (SEQ ID NO: 7270) 270 NVTQ 0.7684 (9/9) +++ (SEQ ID NO: 7271) Residue No. Potential Threshold Assignment Thr 166 0.8547 0.6439 T Thr 367 0.5575 0.5403 T Thr 394 0.8217 0.5821 T Accordingly, the invention comprises a polypeptide comprising a fragment of the amino acid sequence of SEQ ID NO: 6051 wherein said fragment comprises one or more of the N- glycosylation sites identified above. The invention further comprises a polynucleotide encoding one or more of the polypeptides identified above. The invention further comprises a polypeptide comprising a fragment of amino acid sequence SEQ JD NO: 6051 wherein said fragment does not include one or more of the N-glycosylation sites identified above. The invention includes a polynucleotide encoding such a fragment. T-epitopes for SEQ JD NO: 6052 are identified in Table 25. The invention includes a polypeptide for use as an antigen, wherein the polypeptide comprises: (a) an amino acid sequence selected from the group consisting of the T-epitope sequences identified in SEQ JD NOS: 9539-9752; (b) an amino acid sequence having sequence identity to an amino acid sequence of (a). The invention further comprising a polynucleotide sequence encoding the polypeptides of (a) or (b). The invention further comprising a method of expression or delivery of such polynucleotides through viral vectors and/or viral particles. The invention further comprises a polypeptide comprising two or more of the T-epitope sequences identified in SEQ ID NOS: 9539-9752, or a polynucleotide encoding such a polypeptide. A variant of SEQ ID NO: 6052 that is included within the invention is SEQ JD NO: 9964. Compared to SEQ JD NO: 6052, this sequence has Ue at residue 54 instead of Thr. The use as an antigen is preferably a use: (1) as a T-cell antigen; (2) for generating a complex between a class I MHC protein (e.g. a class I HLA) and a fragment of said antigen; (3) as an antigen for raising a cell-mediated immune response; and/or (4) as an antigen for raising a CTL response. The use preferably protects or treats disease and/or infection caused by a SARS virus. The invention provides the use of a polypeptide in the manufacture of a medicament for immunising a mammal (typically a human) against SARS viral infection wherein the polypeptide is as defined above. The invention provides a method of raising an immune response in a mammal (typically a human), comprising the step of administering to the mammal a polypeptide as defined above, wherein said immune response is a cell-mediated immune response and, preferably, a CTL response. The immune response is preferably protective or therapeutic. The invention includes a composition comprising a SARS virus nucleocapsid protein or a fragment thereof and further comprising a SARS virus membrane protein or a fragment thereof. The composition may further comprising one or more adjuvants discussed below. The invention further includes a composition comprising a polypeptide comprising SEQ ID NO: 6051 or a fragment thereof or a sequence having sequence identity thereto and further comprising a polypeptide comprising SEQ JD NO: 6040, or a fragment thereof or a sequence having sequence identity thereto. Such composition may be used, for instance, in a vaccine. Such composition may further comprise one or more adjuvants discussed below. The invention includes a composition comprising a SARS virus nucleocapsid protein or a fragment thereof and a SARS virus spike protein or a fragment thereof. In one embodiment the nucleocapsid protein comprises a polypeptide sequence comprising SEQ JD NO: 6051 or a fragment thereof or a sequence having sequence identity thereto. In one embodiment, the spike protein comprises a polynucleotide comprising SEQ JD NO: 6042 or a fragment thereof or a sequence having sequence identity thereto. The composition may further comprise one or more of the adjuvants discussed below. The invention further includes a composition comprising antibodies specific to a SARS virus nucleocapsid protein and comprising antibodies specific to a SARS virus spike protein. In one embodiment the antibody is specific to a nucleocapsid protein comprises a polypeptide sequence comprising SEQ JD NO: 6051 or a fragment thereof or a sequence having sequence identity thereto. In one embodiment, the antibody is is specific to a spike protein comprises a polynucleotide comprising SEQ JD NO: 6042 or a fragment thereof or a sequence having sequence identity thereto. The invention further includes polynucleotide sequences, and fragments thereof, of a SARS virus which are conserved among coronaviruses, and polypeptides encoded thereby. Such conserved sequences can be identified in the alignments shown in FIGURE 7. Such conserved sequences may be used in the vaccines of the invention or in the diagnostic reagents, kits and methods of the invention. The invention further includes polynucleotide sequences, and fragments thereof, of a SARS virus which are specific to SARS virus and not shared with coronaviruses. Such SARS specific sequences are also identified as SEQ JD NOS: 6040, 6043, 6044, 6047, 6048, 6049 and 6050. Such SARS specific sequences may be used in the vaccines of the invention or in the diagnostic reagents, kits and methods of the invention. The invention also includes polynucleotide sequences which can be used as probes or primers for diagnostic reagents, kits (comprising such reagents) and methods which can be used to diagnose or identify the presence or absence of a SARS virus in a biological sample. The invention includes a polynucleotide sequence comprising one or more of the primer sequences identified inSEQ ID NOS: 6076-6265 (Table 5). The invention further includes polynucleotide sequence comprising the complement of one or more of the primer sequences identified in SEQ JD NOS: 6076-6265. The invention also includes polynucleotide sequences which can be used as probes or primers for diagnostic reagents, kits (comprising such reagents) and methods which can be used to diagnose or identify the presence or absence of a SARS virus in a biological sample. The invention includes a polynucleotide sequence comprising one or more of the primer sequences identified in SEQ ID NOS: 6266-6343 (Table 6). The invention further includes polynucleotide sequence comprising the complement of one or more of the primer sequences identified in SEQ JD NOS: 6266-6343. The invention also includes polynucleotide sequences which can be used as probes or primers for diagnostic reagents, kits (comprising such reagents) and methods which can be used to diagnose or identify the presence or absence of a SARS virus in a biological sample. The invention includes a polynucleotide sequence comprising one or more of the primer sequences identified in SEQ JD NOS: 6344-6392 (Table 7). The invention further includes polynucleotide sequence comprising the complement of one or more of the primer sequences identified in SEQ ID NOS: 6344-6392.. The invention also includes polynucleotide sequences which can be used as probes or primers for diagnostic reagents, kits (comprising such reagents) and methods which can be used to diagnose or identify the presence or absence of a SARS virus in a biological sample. The invention includes a polynucleotide sequence comprising one or more of the primer sequences identified in SEQ ID NOS: 6393-6559 (Tables 8 & 9). The invention further includes polynucleotide sequence comprising the complement of one or more of the primer sequences identified in SEQ ID NOS: 6393-6559. The invention also includes polynucleotide sequences which can be used as probes or primers for diagnostic reagents, kits (comprising such reagents) and methods which can be used to diagnose or identify the presence or absence of a SARS virus in a biological sample. The invention includes a polynucleotide sequence comprising one or more of the primer and probe sequences identified in SEQ JD NOS: 6560-6568. The invention further includes polynucleotide sequence comprising the complement of one or more of the primer sequences identified in SEQ JD NOS: 6560-6568. The invention includes a polypeptide sequence comprising any one of even-numbered SEQ JD NOS: 7272-7290, or a fragment thereof, or a sequence having sequence identity thereto. The invention further includes a polynucleotide sequence encoding any one of even-numbered SEQ JD NOS: 7272-7290, or a fragment thereof, or a sequence having sequence identity thereto. Examples of such polynucleotide sequences are odd-numbered SEQ ID NOS: 7273-7291. The invention includes a polynucleotide sequence comprising an intergenic sequence which is common to each open reading frame of the SARS virus. The SARS virus is thought to use this sequence to signal translation of the open reading frame. The intergenic sequence comprises a lOmer SEQ ID NO: 7292, or optionally a hexamer SEQ ID NO: 7293. When the virus transcribes its positive (+) RNA strand to (-) RNA strand, the virus replicating structure uses the (-) strand template to transcribe nucleotides at the 5' end prior to the first intergenic sequence, followed by the intergenic sequence, followed by the selected open reading frame. The virus then creates multiple mRNAs comprising the 5' end, the intergenic sequence and coding sequence. For more details on Nidovriales replication (including Coronavirus) see e.g., Ziebuhr et al, "Virus-encoded proteinases and proteolytic processing in the Nidovirales", Journal of General Virology 81:853-879 (2000), incorporated herein by reference in its entirety. The invention comprising a polynucleotide sequence comprising SEQ JD NO: 7292 or the complement thereof. The invention comprising a polynucleotide sequence comprising SEQ JD NO: 7293 or the complement thereof. The invention further comprises a polynucleotide sequence comprising nucleotides from the 5' end of the SARS viral genome, or its reverse complement, and further comprising an intergenic sequence or its reverse complement. The polynucleotide may further comprise one or more of the SARS virus open reading frames. Examples of polynucleotide sequences comprising nucleotides from the 5' end of the SARS virus genome followed by the intergenic sequence are SEQ JD NOS: 7294-7301.- The invention includes a polynucleotide sequence comprising a sequence selected from the group consisting of SEQ ID NO: 7292, SEQ JD NO: 7293, SEQ ID NO: 7294, SEQ ID NO: 7295, SEQ ID NO: 7296, SEQ JD NO: 7297, SEQ JD NO: 7298, SEQ JD NO: 7299, SEQ ID NO: 7300 and SEQ ID NO: 7301, or a fragment thereof, or a sequence having sequence identity thereto. In one embodiment, the polynucleotide does not consist entirely of a known SARS virus sequence. The SARS virus intergenic sequence can be used to create a RNAi molecule. Such a SARS virus specific RNAi molecule can be used to treat SARS virus infection. The invention includes a RNAi molecule comprising a double stranded RNA molecule wherein one RNA strand comprises a sequence selected from the group consisting of SEQ JD NO: 7292, SEQ ID NO: 7293, SEQ JD NO: 7294, SEQ ID NO: 7295, SEQ JD NO: 7296, SEQ JD NO: 7297, SEQ JD NO: 7298, SEQ ID NO: 7299, SEQ ID NO: 7300 and SEQ JD NO: 7301, or a fragment thereof. Preferably, said RNA strand comprises a sequence selected from the group consisting of SEQ ID NO: 7292 and SEQ ID NO: 7293. Preferably, the other RNA strand comprises the reverse complement of the first strand or a polynucleotide sequence which hybridizes to the first strand. The invention includes the use of RNAi in a method of treatment for SARS virus infection comprising administering to a mammal an effective amount of the si RNA molecule. Preferably, the RNAi molecule comprises the molecule described above. Further discussion of the RNAi applications of the intergenic sequence is included in section IV of the specification below. The invention also includes the use of a SARS virus antisense nucleotide sequence, preferably antisense directed to the SARS virus intergenic sequence. Such an antisense sequence may be used in the treatment of a subject infected with the SARS virus. The antisense of the SARS virus intergenic sequence can be designed to bind to the SARS viral polynucleotides to block access of the viral replication machinery to the intergenic sequence. Such an antisense sequence may also be used to identify the presence or absence of a SARS virus in a biological sample. The antisence can itself be labeled or the antisense associated with viral polynucleotides can be detected by means known in the art. Antisense nucleic acids are designed to specifically bind to RNA, resulting in the formation of RNA-DNA or RNA-RNA hybrids, with an arrest of DNA replication, reverse transcription or messenger RNA translation. Antisense polynucleotides based on a selected sequence can interfere with expression of the corresponding gene. Antisense polynucleotides will bind and/or interfere with the translation of the corresponding mRNA. The invention also includes the use of the intergenic region with a ribozyme. Trans-cleaving catalytic RNAs (ribozymes) are RNA molecules possessing endoribonuclease activity. Ribozymes are specifically designed for a particular target, and the target message must contain a specific nucleotide sequence. They are engineered to cleave any RNA species site-specifically in the background of cellular RNA. The cleavage event renders the mRNA unstable and prevents protein expression. Importantly, ribozymes can be used to inhibit expression of a gene of unknown function for the purpose of determining its function in an in vitro or in vivo context, by detecting the phenotypic effect. One commonly used ribozyme motif is the hammerhead, for which the substrate sequence requirements are minimal. Design of the hammerhead ribozyme is disclosed in Usman et al., Current Opin. Struct. Biol. (1996) 6:527-533. Usman also discusses the therapeutic uses of ribozymes. Ribozymes can also be prepared and used as described in Long et al., FASEB J. (1993) 7:25; Symons, Ann. Rev. Biochem. (1992) 61:641; Perrotta et al, Biochem. (1992) 31:16- 17; Ojwang et al, Proc. Natl. Acad. Sci. (USA) (1992) 89:10802-10806; and US Patent 5,254,678. Ribozyme cleavage of HJN-I RΝA is described in US Patent 5,144,019; methods of cleaving RΝA using ribozymes is described in US Patent 5,116,742; and methods for increasing the specificity of ribozymes are described in US Patent 5,225,337 and Koizumi et al, Nucleic Acid Res. (1989) 17:7059-7071. Preparation and use of ribozyme fragments in a hammerhead structure are also described by Koizumi et al, Nucleic Acids Res. (1989) 17:7059-7071. Preparation and use of ribozyme fragments in a hairpin structure are described by Chowrira & Burke, Nucleic Acids Res. (1992) 20:2835. Ribozymes can also be made by rolling transcription as described in Daubendiek & Kool, Nat. Biotechnol (1997) 15(3):273-277. The hybridizing region of the ribozyme may be modified or may be prepared as a branched structure as described in Horn & Urdea, Nucleic Acids Res. (1989) 17:6959-67. The basic structure of the ribozymes may also be chemically altered in ways familiar to those skilled in the art, and chemically synthesized ribozymes can be administered as synthetic oligonucleotide derivatives modified by monomeric units. In a therapeutic context, liposome mediated delivery of ribozymes improves cellular uptake, as described in Birikh et al., Eur. J. Biochem. (1997) 245:1-16. Therapeutic and functional genomic applications of ribozymes proceed beginning with knowledge of a portion of the coding sequence of the gene to be inhibited. In the present invention, the target sequence preferably comprises the intergeneic sequence of the SARS virus. Preferably, the sequence is selected from the group consisting of SEQ ID NO: 7292 and SEQ JD NO: 7293. A target cleavage site is selected in the target sequence, and a ribozyme is constructed based on the 5' and 3' nucleotide sequences that flank the cleavage site. Preferably, the 5' nucleotide sequence includes the 5' untranslated region of the SARS virus. The ribozyme may then further be constructed from one or more of the polynucleotide sequences selected from the group consisting of SEQ ID NO: 7294, SEQ ID NO: 7295, SEQ JD NO: 7296, SEQ ID NO: 7297, SEQ JD NO: 7298, SEQ JD NO: 7299, SEQ ID NO: 7300 and SEQ JD NO: 7301. Antisense treatment of HJN infection is described in the following references, each of which is incorporated herein by reference in their entirety, (antisense RΝA complementary to the mRΝA of gag, tat, rev, env) (Sezakiel et al, 1991, J. Virol. 65:468-472; Chatterjee et al, 1992, Science 258:1485-1488; Rhodes et al, 1990, J. Gen. Virol. 71:1965. Rhodes et al, 1991, AIDS 5:145-151; Sezakiel et al, 1992, J. Virol. 66:5576-5581; Joshi et al, 1991, J. Virol. 65:5524-5530). The invention includes the use of decoy RNA to disrupt the SARS virus replication and life cycle. Methods of making and using such decoy RNA for treatment of a viral infection are known in the art. The invention includes delivery of genes encoding, for example, the SARS virus intergenic sequence, to infected cells. Preferably, the sequence comprises one or more of the sequences selected from the group consisting of SEQ JD NO: 7292, SEQ ID NO: 7293, SEQ ID NO: 7294, SEQ ID NO: 7295, SEQ JD NO: 7296, SEQ ID NO: 7297, SEQ JD NO: 7298, SEQ ID NO: 7299, SEQ JD NO: 7300 and SEQ JD NO: 7301. Preferably, the sequence comprises one or more of the sequences selected from the group consisting of SEQ JD NO: 7292 and SEQ ID NO: 7293. Preferably, the sequence comprises SEQ JD NO: 7293. In the present invention, delivery of intergenic sequence which is not linked to the SARS virus open reading frames disrupts the translation process of the viral RNA and decreases the production of vial proteins. Similar methods of treatment for HIV viral infection have been described. The following references discuss the use of decoy RNA of HJN TAR or RRE for treatment of HIV infection. Each of these references is incorporated herein by reference in their entirety. (Sullenger et al, 1990, Cell 63:601-608; Sullenger et al, 1991, J. Virol. 65:6811-6816; Lisziewicz et al, 1993, New Biol. 3:82-89; Lee et al, 1994, J. Virol. 68:8254-8264), ribozymes (Sarver et al, 1990, Science 247:1222-1225; Wecrasinghe et al, 1991, J. Virol. 65:5531-5534; Dropulic et al. , 1992, J. Virol. 66: 1432-1441 ; Ojwang et al , 1992, Proc. Natl. Acad. Sci. USA. 89:10802-10806; Yu et al, 1993, Proc. Natl. Acad. Sci. USA. 90:6340-6344; Yu et al, 1995, Proc. Natl. Acad. Sci. USA. 92:699-703; Yamada et al, 1994, Gene Therapy 1:38-45). The invention includes the use of the SARS virus intergenic sequence in diagnostic reagents, kits (comprising such reagents) and methods which can be used to diagnose or identify the presence or absence of a SARS virus in a biological sample. Such diagnostic reagents, kits, and methods are further discussed in Section JJ of the specification. The invention includes a pair of primers for amplifying a SARS polynucleotide sequence comprising (i) a first primer comprising a sequence which is substantially identical to a portion of a sequence selected from the group consisting of SEQ JD NO: 7292, SEQ JD NO: 7293, SEQ JD NO: 7294, SEQ JD NO: 7295, SEQ JD NO: 7296, SEQ JD NO: 7297, SEQ JD NO: 7298, SEQ JD NO: 7299, SEQ ID NO: 7300 and SEQ ID NO: 7301 and (ii) a second primer comprising a sequence which is substantially complementary to a portion of a sequence selected from the group consisting of the sequence SEQ JD NO: land the sequence SEQ ID NO: 2, such that the primer pair (i) and (ii) defines a template sequence within a sequence from the group consisting of the sequence SEQ LD NO: land the sequence SEQ ID NO: 2. Preferably, the (i) first primer comprises a sequence which is substantially identical to a portion of a sequence selected from the group consisting of SEQ ID NO: 7292 and SEQ JD NO: 7293. Preferably, the (i) first primer comprises a sequence which is substantially identical to a portion of the sequence of SEQ JD NO: 7293. The amplicon defined by said first and second primers is preferably between 50 and 250 nucleotides in length. The primers may optionally be labeled to facilitate their detection. Methods and compositions for use in labeling primers are discussed further in the application in Section UI. The invention further includes a pair of primers for amplifying a SARS polynucleotide sequence comprising (i) a first primer comprising a sequence which is substantially identical to a portion of the complement of a portion of a sequence selected from the group consisting of SEQ ID NO: 7292, SEQ JD NO: 7293, SEQ JD NO: 7294, SEQ ID NO: 7295, SEQ JD NO: 7296, SEQ JD NO: 7297, SEQ JD NO: 7298, SEQ ID NO: 7299, SEQ ID NO: 7300 and SEQ JD NO: 7301 and (ii) a second primer comprising a sequence which is substantially complementary to a portion of the complement of a sequence selected from the group consisting of the sequence SEQ ID NO: land the sequence SEQ JD NO: 2, such that the primer pair defines a template sequence within a sequence selected from the group consisting of the sequence SEQ ID NO: 1 and the sequence SEQ JD NO: 2. The amplicon defined by said first and second primers is preferably between 50 and 250 nucleotides in length. The primers may optionally be labeled to facilitate their detection.. Methods and compositions for use in labeling primers are discussed further in the application in Section III. , The invention includes a kit comprising (i) a first primer comprising a sequence which is substantially identical to a portion of a sequence selected from the group consisting of SEQ ID NO: 7292, SEQ JD NO: 7293, SEQ JD NO: 7294, SEQ JD NO: 7295, SEQ ID NO: 7296, SEQ JD NO: 7297, SEQ JD NO: 7298, SEQ ID NO: 7299, SEQ JD NO: 7300 and SEQ JD NO: 7301 and (ii) a second primer comprising a sequence which is substantially complementary to a portion of a sequence selected from the group consisting of the sequence SEQ ID NO: 1 and the sequence SEQ JD NO: 2, such that the primer pair (i) and (ii) defines a template sequence within a sequence from the group consisting of SEQ JD NO: 1 and SEQ ID NO: 2. Preferably, the (i) first primer comprises a sequence which is substantially identical to a portion of a sequence selected from the group consisting of SEQ ID NO: 7292 and SEQ JD NO: 7293. Preferably, the (i) first primer comprises a sequence which is substantially identical to a portion of the sequence of SEQ ID NO: 7293. The primers may optionally be labeled to facilitate their detection. Methods and compositions for use in labeling primers are discussed further in the application in Section UI. Other preferred kits comprise (i) a first primer comprising a sequence which is substantially identical to a portion of the complement of a portion of a sequence selected from the group consisting of SEQ ID NO: 7292, SEQ ID NO: 7293, SEQ ID NO: 7294, SEQ JD NO: 7295, SEQ ID NO: 7296, SEQ JD NO: 7297, SEQ ID NO: 7298, SEQ JD NO: 7299, SEQ JD NO: 7300 and SEQ ID NO: 7301 and (ii) a second primer comprising a sequence which is substantially complementary to a portion of the complement of a sequence selected from the group consisting of SEQ ID NO: 1 and SEQ JD NO: 2, such that the primer pair defines a template sequence within a sequence selected from the group consisting of SEQ JD NO: 1 and SEQ ID NO: 2. The invention further includes an attenuated SARS virus for use as a vaccine wherein the intergenic region has been mutated to reduce expression of the viral structural or nonstructural proteins. The attenuated SARS virus may comprises one or more additions, deletions or insertion in one or more of the intergenic regions of the viral genome. Preferably, the attenuated SARS virus comprises an addition, deletion or insertion in one or more occurrences of the sequence selected from the group consisting of SEQ JD NO: 7292 and SEQ ID NO: 7293. Preferably, the addition, deletion or insertion occurs in one or more occurrences of SEQ JD NO: 7293. The invention further comprises a small molecule which inhibits binding or association of the SARS viral replication machinery, such as a ribonucleoprotein, with the intergenic region of the viral genome. Preferably, the small molecule inhibits binding or association of the SARS viral machinery with a sequence selected from the group consisting of SEQ ID NO: 7292 and SEQ JD NO: 7293. Preferably, the small molecule inhbiits binding or association of the SARS viral machinery with SEQ ID NO: 7293. The invention further includes a method of screening for a small molecule for treatment of SARS viral infection comprising using an assay to identify a small molecule which interferes with the association of the SARS viral replication machinery with the intergenic region of the SARS viral genome. The invention further provides a novel SARS polynucleotide sequence SEQ ID NO: 9968. All six reading frames of this 690mer sequence are shown in Figure 113. The constituent amino acid sequences from Figure 113, having at least 4 amino acids, are listed as SEQ JD NOS: 9969 to 10032. Accordingly the invention includes a polynucleotide sequence comprising SEQ ID NO: 9968. It also provides polynucleotide sequences having sequence identity to SEQ JD NO: 9968. The degree of sequence identity is preferably greater than 50% (e.g., 60%, 70%, 80%, 85%, 88%, 90%, 92%o, 95%, 99% or more). The invention includes an amino acid sequence encoded by the polynucleotide sequence of SEQ JD NO: 9968, including the amino acid sequences selected from the group consisting of SEQ ID NO s : 9969 to 10032. Preferably, the amino acid sequence comprises SEQ ID NO: 9997 or comprises SEQ JD NO: 9998. The invention also provides amino acid sequences having sequence identity to an amino acid sequence encoded by SEQ ID NO: 9968. The invention provides amino acids having sequence identity to an amino acid sequence selected from the group consisting of SEQ JD NO : 9969 to 10032. The degree of sequence identity is preferably greater than 50% (e.g., 60%, 70%, 80%, 85%, 88%, 90%, 92%, 95%, 99% or more). A portion of SEQ JD NO: 9968 matches with approximately 98% identity to a previously published SARS polynucleotide sequence, commonly referred to as "BNI-1" (SEQ ID NO: 10033). BNI-1 was sequenced at Bernhard Nocht Institute for Tropical Medicine, National Reference Center for Tropical Infectious Diseases in Hamburg, Germany. The BNI-1 sequence was published on the WHO website on April 4, 2003 at http://www.who.int/csr/sars/primers/en and in Dorsten et al, "Identification of a Novel Coronavirus in Patients with Severe Acute Respiratory Syndrome", New England Journal of Medicine, published online at http://www.nejm.org on April 10, 2003. Both references are incorporated herein by reference in their entirety. The six reading frames of this 302mer sequence are shown in Figure 114 (see also Figure 129). The constituent amino acid sequences from Figure 114, having at least 4 amino acids, are listed as SEQ JD NO s : 10034 to 10065. An alignment of SEQ JD NO: 10034 with SEQ JD NO: 9997 is shown in Figure 130: The invention provides for polynucleotide sequences comprising fragments of SEQ JD NO: 9968. In one embodiment, the fragment does not consist entirely of SEQ ID NO: 10033 or of a known coronavirus. The invention provides for amino acid sequences comprising fragments of an amino acid sequence encoded by SEQ JD NO: 9968. In one embodiment, the fragment does not consist entirely of an amino acid sequence encoded by SEQ ID NO: 10033 or a known coronavirus. The invention provides for amino acids comprising fragments of an amino acid sequence selected from the group consisting of SEQ JD NO : 9969 to 10032. In one embodiment, the fragment does not consist entirely of an amino acid sequence encoded by the polynucleotide sequence of SEQ JD NO: 10033 or a known coronavirus. Approximately 100 nucleotides at the 5' end of SEQ JD NO: 9968 do not match any portion of the BNI-1 polynucleotide sequence (SEQ JD NO: 10033). This unmatched portion is set forth as SEQ ID NO: 10066. The invention thus further provides a polynucleotide comprising the sequence comprising SEQ ID NO: 10066, polynucleotide sequences having sequence identity to SEQ JD NO: 10066, or polynucleotide sequences comprising fragments of SEQ ID NO: 10066. The invention further comprises an amino acid sequence encoded by SEQ ID NO: 10066, an amino acid sequence having sequence identity to an amino acid sequence encoded by SEQ JD NO: 10066, or an amino acid sequence comprising fragments of an amino acid sequence encoded by SEQ ID NO: 10066. Preferably, the amino acid sequence comprises SEQ ID NO: 10067. SEQ JD NO: 9997/9998 demonstrates homology with the a region of pollab of several coronaviruses. FIGURE 115 shows an alignment of SEQ ID NO s : 9997/9998 to amino acid sequences for pollab of bovine coronavirus (SEQ ID NO: 10068), avian infectious bronchitis virus (SEQ ID NO: 10069) and murine hepatitis virus (SEQ ID NO: 10070). A consensus amino acid sequence of SEQ ID NO s : 9997/9998, SEQ ID NO: 10068, SEQ JD NO: 10069, and SEQ ID NO: 10070 is shown in the bottom row of the alignment in Figure 115 (e.g. SEQ ID NO: 10071). As shown in FIGURE 113, the polynucleotide sequence encoding SEQ ID NO: 9997 has a stop codon after codon 205, between SEQ ID NO s : 9997 and 9998. Optionally, the stop codon can be removed and the amino acid sequence continued (SEQ ID NO: 10072). Accordingly, the invention provides for an amino acid sequence comprising SEQ JD NO: 9997 and/or SEQ JD NO: 9998, or SEQ ID NO: 10072, and further comprising an amino acid sequence encoding for the C-terminus of a coronavirus pollab gene or a fragment thereof. As shown in FIGURE 115, SEQ JD NO s : 10068, 10069, 10070 and 10071 contain amino acids prior to the N-terminus of SEQ JD NO: 9997. The invention also provides for an amino acid sequence comprising SEQ ID NO: 9997 and further comprising an amino acid sequence encoding for the N-terminus of a coronavirus pollab protein or a fragment thereof. The pollab sequences on FIGURE 115 contain a coding region indicated on the schematic of FIGURE 117 by a "*". In FIGURE 115, the beginning of this genomic region is designated by the arrow crossing in front of amino acid 6080 of the consensus sequence SEQ JD NO: 10071. The end of this genomic region is designated by the arrow crossing in front of amino acid 6604 of the consensus sequence. The invention provides for an amino acid sequence comprising SEQ JD NO: 9997 and/or SEQ ID NO: 9998, or SEQ ID NO: 10072, and further comprising a first amino sequence prior to the N-terminus of said SEQ ID NO: 9997 and/or SEQ ID NO: 9998, or SEQ ID NO: 10072, wherein said first amino acid sequence has homology to an N-terminus sequence of a known coronavirus pollab "*" protein or a fragment thereof. The invention further provides for an amino acid sequence comprising SEQ JD NO: 9997 and SEQ JD NO: 9998, wherein the stop codon after SEQ ID NO: 9971 is removed (i.e. SEQ JD NO: 10072), and further comprising a second amino acid sequence following the C terminus of SEQ ID NO: 9998, wherein said second amino acid sequence is homologous with a C terminus of a known coronavirus pollab "*" protein or a fragment thereof. Examples of such proteins are shown aligned in FIGURE 118, and are SEQ ID NO s : 10073 to 10077. SEQ JD NO: 10073 comprises SEQ ID NO: 9997 and further comprises amino acids prior to the N-terminus and subsequent to the C-terminus from the pollab "*" protein of avian infectious bronchitis virus. SEQ ID NO: 10074 comprises SEQ JD NO: 9997 and further comprises amino acids prior to the N-terminus and subsequent to the C-terminus from the pollab "*" protein of bovine coronavirus. SEQ ID NO: 10075 comprises SEQ JD NO: 9997 and further comprises amino acids prior to the N-terminus and subsequent to the C-terminus from the pollab "*" protein of murine hepatitis virus. SEQ ID NO: 10076 comprises SEQ ID NO: 9997 and further comprises amino acids prior to the N-terminus and subsequent to the C-terminus from the consensus of the pollab "*" protein of avian infectious bronchitis virus, bovine coronavirus, and murine hepatitis virus (FIGURE 115). SEQ ID NO: 10077 comprises the consensus sequence of SEQ ID NOS : 10073 to 10076. The invention comprises an amino acid sequence selected from the group consisting of SEQ JD NO s : 10073, 10074, 10075, 10076 and 10077. The invention further includes an amino acid sequence comprising fragments of an amino acid sequence selected from the group consisting of SEQ JD NO s : 10073,40074, 10075, 10076 and 10077. The invention further comprises an amino acid sequence with sequence identity to a sequence selected from the group consisting of SEQ JD NO s : 10073, 10074, 10075, 10076 and 10077. The invention comprises polynucleotides encoding for the amino acid sequences selected from the group consisting of SEQ JD NO s : 10073, 10074, 10075, 10076 and 10077. The invention comprises polynucleotides having sequence identity to polynucleotides encoding for the amino acid sequences selected from the group consisting of SEQ ID NO : 10073, 10074, 10075, 10076 and 10077. The invention comprises fragments of polynucleotides encoding SEQ JD NO s : 10073, 10074, 10075, 10076 and 10077. As shown in Figure 113, SEQ ID NO: 9968 includes a sequence that encodes SEQ ID NO: 10020 followed by a stop codon, giving a C-terminus threonine (Thr) residue. The corresponding sequence from an amino acid sequence encoded by BNI-1 is SEQ JD NO: 10078, which continues past the C-terminus of SEQ ID NO: 10020. Accordingly, the invention includes a protein comprising amino acid sequence SEQ JD NO: 10020 or an amino acid sequence having sequence identity to SEQ JD NO: 10020 or an amino acid sequence comprising a fragment of SEQ ID NO: 10020, wherein the C-terminus residue of said protein is a threonine. Preferably, the C-terminus of said protein is -ST. Still more preferably, the C-terminus of said protein is - EST. The invention also includes a protein comprising amino acid sequence SEQ ID NO: 10078 or an amino acid sequence having sequence identity to SEQ JD NO: 10078 or an amino acid sequence comprising a fragment of SEQ JD NO: 10078, wherein the C-terminus residue of said protein is Thr. Preferably, the C-terminus of said protein is -ST. Still more preferably, the C- terminus of said protein is -EST. SEQ ID NO: 9968 also encodes a 54mer amino acid sequence SEQ JD NO: 10015. The polynucleotide encoding SEQ JD NO: 10015 encodes two stop codons at its C-terminus (Figure 113). The corresponding region from the BNI-1 sequence does not contain this 54mer. Accordingly, the invention includes a protein comprising amino acid sequence SEQ ID NO: 10015, or an amino acid sequence having sequence identity to SEQ JD NO: 10015 or an amino acid sequence comprising a fragment of SEQ ID NO: 10015. The invention further includes a polypeptide comprising SEQ ID NO: 10015 and further comprising a first amino acid sequence prior to the N-terminus of SEQ JD NO: 10015. SEQ ID NO: 9968 encodes the amino acid sequence SEQ ID NO: 9969. The polynucleotide sequence contains a stop codon at the C-terminus of SEQ ID NO: 9969. Accordingly, the invention includes a protein comprising amino acid sequence SEQ JD NO: 9969, or an amino acid sequence having sequence identity to SEQ JD NO: 9969. The invention further includes a polypeptide comprising SEQ JD NO: 9969 and further comprising a first amino acid sequence prior to the N-terminus of SEQ JD NO: 9969. The invention further includes a polypeptide comprising the sequence SEQ ID NO: 10079. SEQ JD NO: 9968 encodes amino acid sequence QRT (Figure 113), followed by a stop codon. Accordingly, the invention includes a protein comprising amino acid sequence QRT. The invention further includes a polypeptide comprising amino acid sequence QRT and further comprising a first amino acid sequence prior to the N-terminus of the sequence QRT. SEQ ID NO: 9968 encodes amino acid sequence SEQ ID NO: 10022, followed by a stop codon at its C-terminus. Accordingly, the invention includes a protein comprising amino acid sequence SEQ ID NO: 10022, or an amino acid sequence having sequence identity to SEQ ID NO: 10022. The invention further includes a polypeptide comprising SEQ ID NO: 10022 and further comprising a first amino acid sequence prior to the N-terminus of SEQ JD NO: 10022. SEQ JD NO: 9968 encodes amino acid sequence SEQ JD NO: 10027. Within the SEQ ID NO: 10027 coding sequence there are at least three start codons, identified with underlining in Figure 119. The open reading frame indicated by the first start codon is SEQ JD NO: 10081. The open reading frame indicated by the second start codon is SEQ JD NO: 10082. The open reading frame indicated by the third start codon is SEQ ID NO: 10083. The invention provides a novel SARS polynucleotide sequence SEQ ID NO: 10084. All six reading frames of this 1463mer sequence are shown in Figure 120 (see also Figure 122). The constituent amino acid sequences from Figure 120, having at least 4 amino acids, are listed as SEQ ID NOS: 10085 to 10209 (see Figures 120A to 120F). The invention includes a polynucleotide sequence comprising SEQ JD NO: 10084. The invention also provides polynucleotide sequences having sequence identity to SEQ JD NO: 10084. The invention also provides for polynucleotide sequences comprising fragments of SEQ ID NO: 10084. In one embodiment, the polynucleotide fragment does not consist entirely of SEQ JD NO: 10033 or a known coronavirus polynucleotide sequence or a known SARS polynucleotide sequence. The invention includes an amino acid sequence encoded by the polynucleotide sequence of SEQ ID NO: 10084, including the amino acid sequences of Figures 120A to 120F e.g. selected from the group consisting of SEQ ID NO : 10085 to 10209. Preferably, the amino acid sequence comprises SEQ JD NO: 10149. The invention also provides amino acid sequences having sequence identity to an amino acid sequence encoded by SEQ ID NO: 10084. The invention provides amino acids having sequence identity to an amino acid sequence from Figures 120 A to 120F e.g. selected from the group consisting of SEQ ID NO s : 10085 to 10209. ' The invention also provides fragments of amino acid sequences encoded by SEQ ID NO: 10084. The invention also provides fragments of amino acid sequences selected from the group consisting of SEQ ID NO s : 10085 to 10209. In one embodiment, the fragment does not consist entirely of an amino acid sequence encoded by SEQ JD NO: 10033 or an amino acid sequence of a known coronavirus or an amino acid sequence of a known SARS virus. An alignment of the matching portion of SEQ JD NO: 10033 and SEQ ID NO: 10084 is included in FIGURE 121. In one embodiment, the invention comprises an amino acid sequence comprising SEQ ID NO: 10149. An alignment of the polynucleotide sequence SEQ JD NO: 10084 to the encoded SEQ ID NO: 10149 is shown in FIGURE 122 (5'3' Frame 3). Analysis of the 5'3' Frame 3 translation by a computer program to predict start codon methionines (NetStart 1.0) (FIGURE 123) reveals SEQ ID NO s : 10210 to 10215. The invention includes a protein comprising an amino acid sequence selected from the group consisting of SEQ JD NO: 10210, SEQ ID NO: 10211, SEQ ID NO: 10212, SEQ JD NO: 10213, SEQ JD NO: 10214 and SEQ ID NO: 10215. The invention includes a protein having sequence identity to an amino acid sequence selected from the group consisting of SEQ ID NO: 10210, SEQ ID NO: 10211, SEQ JD NO: 10212, SEQ ID NO: 10213, SEQ ID NO: 10214 and SEQ ID NO: 10215. In one embodiment, the protein does not consist entirely of an amino acid sequence of a known SARS virus or of a known coronavirus. The invention includes a fragment of a protein comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 10210, SEQ JD NO: 10211, SEQ ID NO: 10212, SEQ JD NO: 10213, SEQ ID NO: 10214 and SEQ JD NO: 10215. In one embodiment, the fragment does not consist entirely of an amino acid sequence of a known SARS virus or of a known coronavirus. In one embodiment, the invention includes a polypeptide comprising the amino acid sequence selected from the group consisting of SEQ JD NO: 10210, SEQ ID NO: 10211 and SEQ ID NO: 10212. Partial results of a BLAST of SEQ JD NO: 10210 against GenBank is included in FIGURE 124. These results indicate that SEQ JD NOS: 10210, 10211 and 10212 have functional similarities to a Coronavirus RNA polymerase, particularly the RNA polymerase of murine hepatitis virus, bovine coronavirus, and avian infectious bronchitis. In one embodiment, the invention is directed to a polypeptide comprising a first amino acid sequence selected from the group consisting of SEQ ID NO: 10210, SEQ ID NO: 10211 and SEQ JD NO: 10212 and a second amino acid sequence from the C-terminus of a coronavirus ORFlab sequence. Preferably, the second amino acid sequence is from a bovine coronavirus. One example of this embodiment is shown below as SEQ JD NO: 10216. Amino acids 1-481 of SEQ JD NO: 10216 are the first amino acid sequence of SEQ JD NO: 10210, and amino acids 482-1152 are the second amino acid sequence of the C-terminus of a bovine coronavirus orf lab polyprotein (Gi 26008080) (NP_150073.2) (SEQ JD NO: 10217). Accordingly, the invention includes a polypeptide comprising SEQ JD NO: 10216. The invention further includes a polypeptide comprising a first amino acid sequence of SEQ ID NO: 10210 and a second amino acid sequence of SEQ JD NO: 10217. The invention further includes a polypeptide comprising a first amino acid sequence having greater than x% identity to SEQ ID NO: 10210 and a second amino acid sequence having greater than y% identity to SEQ ID NO: 10217, wherein x is greater than or equal to 85% (e.g., 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more) and wherein y is greater than or equal to 60% (e.g., 65%, 70%, 75%, 80%, 85%, 90%, 95%, 98%, 99% or more). The invention also includes a polypeptide comprising a fragment of SEQ ID NO: 10210, wherein said fragment includes an epitope. Computer-predicted epitopes of SEQ ID NO: 10210, using a 17mer window, are included in FIGURE 125A (Hopp & Woods) and FIGURE 125B (Kyte & Doolittle). The amino acid sequence of SEQ ID NO: 10210 also contains two predicted glycosylation sites at amino acids 81-84 (NNTE; SEQ JD NO: 10218) and at 180-183 (NHSV; SEQ ID NO: 10219). Accordingly, the invention includes a polypeptide comprising a fragment of SEQ JD NO: 10210, wherein said fragment includes a glycosylation site. The invention further includes a polypeptide comprising a fragment of SEQ JD NO: 10210, wherein said fragment includes the Asn at position 81. Preferably, said Asn is glycosylated. The invention further includes a polypeptide comprising a fragment of SEQ ID NO: 10210, wherein said fragment includes the Asn at position 180. Preferably, said Asn is glycosylated. In one embodiment, the invention includes a polypeptide comprising an amino acid sequence from within Figure 120D and/or SEQ JD NO s : 10150 to 10160 e.g. from SEQ JD NO s : 10154, 10155, 10158 and 10160. Within SEQ JD NO: 10154 the following amino acid sequences starting with a Met and ending at a stop codon can be identified: SEQ ID NO s : 10220 to 10227. Accordingly, the invention includes a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 10220, SEQ ID NO: 10221, SEQ ID NO: 10222, SEQ JD NO: 10223, SEQ ID NO: 10224, SEQ ID NO: 10225, SEQ JD NO: 10226 and SEQ JD NO: 10227, or a fragment thereof or an amino acid sequence having sequence identity thereto. In one embodiment, the invention includes a polypeptide comprising the amino acid sequence within Figure 120E e.g. from SEQ ID NO s : 10161 to 10182, and in particular SEQ ID NOS: 10171 and 10176. Within SEQ ID NO s : 10171 and 10176 the following amino acid sequences starting with a Met and ending at a stop codon can be identified: SEQ ID NO: 10228 and SEQ ID NO: 10229. Accordingly, the invention includes a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 10228 and SEQ ID NO: 10229, or a fragment thereof or an amino acid sequence having sequence identity thereto. In one embodiment, the invention includes a polypeptide comprising an amino acid sequence from Figure 120F e.g. SEQ JD NO s : 10183 to 10209. Within Figure 120F the following amino acid sequence starting with a Met and ending at a stop codon can be identified: SEQ JD NO: 10187. Accordingly, the invention includes a polypeptide comprising an amino acid sequence of SEQ ID NO: 10187, or a fragment thereof or an amino acid sequence having sequence identity thereto. In one embodiment, the polynucleotides of the invention do not include one of the following primers, disclosed at http://content.nejm.org/cgi/reprint/NEJMoa030781v2.pdf. 5 ' GGGTTGGGACTATCCTAAGTGTGA3 ' (SEQ ID NO: 10230) 5 ' TAACACACAACICCATCATCA3 ' (SEQ ID NO: 10231) 5 ' CTAACATGCTTAGGATAATGG3 ' (SEQ ID NO: 10232) 5 ' GCCTCTCTTGTTCTTGCTCGC3 ' (SEQ ID NO: 10233) 5 ' CAGGTAAGCGTAAAACTCATC3 ' (SEQ ID NO: 10234) The invention also includes polynucleotide sequences which can be used as probes for diagnostic reagents, kits (comprising such reagents) and methods which can be used to diagnose or identify the presence or absence of a SARS virus in a biological sample. The invention includes the polynucleotide primers identified in Table 31 (SEQ JD NO s : 10235 to 10258), the forward primers SEQ ID NO s : 10259 to 10281 and the reverse primers SEQ JD NO s : 10282 to 10298. The invention further includes polynucleotide sequences which are complementary to any one of these primer sequences disclosed herein. The invention provides a SARS polynucleotide sequence SEQ JD NO: 10299. All six reading frames of this sequence are included in FIGURE 126 (See also Figure 131). The constituent amino acid sequences from Figure 126, having at least 4 amino acids, are listed as SEQ ID NOS: 10300 to 10337. Accordingly, the invention includes a polynucleotide sequence comprising SEQ ID NO: 10299. It also provides polynucleotide sequences having sequence identity to SEQ JD NO: 10299. The invention also provides for polynucleotide sequences comprising fragments of SEQ ID NO: 10299. In one embodiment, the polynucleotide fragment does not consist entirely of a known polynucleotide sequence of a SARS virus or a known polynucleotide sequence of a coronavirus. The invention includes an amino acid sequence encoded by the polynucleotide sequence of SEQ ID NO: 10299, including the amino acid sequences shown in Figure 126, and the amino acid sequences selected from the group consisting of SEQ JD NO : 10300 to 10337. Preferably, the amino acid sequence comprises SEQ JD NO: 10316. The invention also provides amino acid sequences having sequence identity to an amino acid sequence encoded by SEQ JD NO: 10299. The invention provides amino acid sequences having identity to an amino acid sequence selected from the group consisting of SEQ JD NO : 10300 to 10337. ' The invention also provides fragments of amino acid sequences encoded by SEQ ID NO: 10299. The invention also provides fragments of amino acid sequences selected from the group consisting of SEQ ID NO : 10300 to 10337. In one embodiment, the fragment does not consist entirely of a known amino acid sequence of a SARS virus or a known amino acid sequence of a coronavirus. In one embodiment, the invention comprises an amino acid sequence comprising SEQ JD NO: 10316. Encoded open reading frames within SEQ JD NO: 10316 include SEQ JD NO: 10338 and SEQ ID NO: 10339. In one embodiment, the invention comprises an amino acid sequence comprising a sequence from within the 5'3' Frame 1 translation of SEQ ID NO: 10299. The following encoded open reading frame is found within this translation: SEQ ID NO: 10340. In one embodiment, the invention comprises an amino acid sequence comprising a sequence from within the 3 '5' Frame 1 translation of SEQ JD NO: 10299. An encoded open reading frame within this translation is SEQ ID NO: 10341. In one embodiment, the invention comprises an amino acid sequence comprising a sequence from within the 3'5' Frame 2 translation of SEQ ID NO: 10299. An encoded open reading frame within this franslation is SEQ JD NO: 10342. The invention includes a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ JD NO: 10338, SEQ ID NO: 10339, SEQ ID NO: 10340, SEQ ID NO: 10341 and SEQ JD NO: 10342. The invention includes a polypeptide having sequence identity to an amino acid sequence selected from the group consisting of SEQ JD NO: 10338, SEQ JD NO: 10339, SEQ JD NO: 10340, SEQ ID NO: 10341 and SEQ JD NO: 10342. The invention includes a fragment of a polypeptide comprising an amino acid sequence elected from the group consisting of SEQ ID NO: 10338, SEQ JD NO: 10339, SEQ ID NO: 10340, SEQ ID NO: 10341 and SEQ JD NO: 10342. In one embodiment, the fragment does not consist entirely of a known SARS virus amino acid sequence or of a known coronavirus amino acid sequence. 5 In one embodiment, SEQ ID NOS: 10338-10342 are used in fusion proteins. Accordingly, the start codon methionines may be removed. The invention comprises a amino acid sequence selected from the group consisting of SEQ ID NO: 10343, SEQ ID NO: 10344, SEQ ID NO: 10345, SEQ ID NO: 10346 and SEQ ID NO: 10347. In one embodiment, the invention comprises an amino acid sequence selected from the 0 group consisting of SEQ ID NO: 10338 and SEQ ID NO: 10339. Partial BLAST results of SEQ JD NO: 10338 against GenBank are given below: >gi 1133593 | sp|P18457 |RRPB_CVPFS RNA-DIRECTED RNA POLYMERASE (ORFlB) gi|93934|pirj |A43489 RNA-directed RNA polymerase (EC 2.7.7.48) - porcine transmissible gastroenteritis virus (fragment) L5 gi I 833161 |emb]CAA37284.11 polymerase [Transmissible gastroenteritis virus] Length = 533 Score = 131 bits (329), Expect = 3e-30 ',0 Identities = 55/89 (61%), Positives = 69/89 (77%), Gaps = 1/89 (1%) Query: 1 . MLWCKDGHVΞTFYPKLQASQAWQPGVAMPNLYKMQRMLLEKCDLQNYGENAVIPKGIMMN 60 MLWC++ H++TFYP+LQ+++ W PG +MP LYK+QRM LE+C+L NYG +P GI N Sbjct: 217 MLWCENSHIKTFYPQLQSAE-WNPGYSMPTLYKIQRMCLERCNLYNYGAQVKLPDGITTN 275 5 Query : 61 VAKYTQLCQYLNTLTLAVPSNMRVIHFGA 89 V KYTQLCQYLNT TL VP MRV+H GA Sbj ct : 276 WKYTQLCQYLNTTTLCVPHKMRVLHLGA 304 0 These results indicate that SEQ JD NO: 10338 has functional similarities to an RNA- directed RNA polymerase of porcine transmissible gastroenteritis virus. Partial BLAST results of SEQ JD NO: 10339 against GenBank are given below: >gb | AAL57305 . 1 1 replicase [bovine coronavirus ] Length = 7094 5 Score = 139 bits ( 351 ) , Expect = 7e-33 Identities = 64 / 108 ( 59 % ) , Positives = 78 / 108 ( 72 % ) Query : 1 MSVISKWKVTIDYAEISFMLWCKDGHVETFYPKLQASQAWQPGVAMPNLYKMQRMLLEK 60 ) M+ +SKW V +D+ + FMLWC D V TFYP+LQA+ W+PG +MP LYK +E+ Sbj ct : 6760 LNCVSKVVNVNVDFKDFQFMLWCNDEKVMTFYPRLQAASDWKPGYSMPVLYKYLNSPMER 6819 Query : 61 CDLQNYGENAVIPKGIMMNVAKYTQLCQYLNTLTLAVPSNMRVIHFGA 108 i L NYG+ +P G MMNVAKYTQLCQYLNT TLAVP NMRV+H GA Sbj ct : 6820 VSLWNYGKPVTLPTGCMMNVAKYTQLCQYLNTTTLAVPVNMRVLHLGA 6867 These results indicate that SEQ ID NO: 10339 has functional similarities to a replicase of bovine coronavirus. The SARS virus may contain polymorphism at the Glu-20 residue of SEQ JD NO: 10338. The invention includes a polypeptide comprising an amino acid sequence having sequence identity to SEQ ID NO: 10338, wherein said polypeptide includes an amino acid sequence selected from the group consisting of ASQAW (SEQ ID NO: 10348) and ASRAW (SEQ ID NO: 10349). The invention includes a fragment of a polypeptide comprising SEQ ID NO: 10338, wherein said fragment includes an amino acid sequence selected from the group consisting of SEQ JD NO: 10348 and SEQ ID NO: 10349. The SARS virus may contain polymorphism at the Ser-80 residue of SEQ JD NO: 10338. below. The invention includes a polypeptide comprising an amino acid sequence having sequence identity to SEQ JD NO: 10338, wherein said polypeptide includes an amino acid sequence selected from the group consisting of VPSNM (SEQ ID NO: 10350) and VPTNM (SEQ JD NO: 10351). The invention includes a fragment of a polypeptide comprising SEQ ID NO: 10338, wherein said fragment includes an amino acid sequence selected from the group consisting of SEQ JD NO: 10350 and SEQ JD NO: 10351. The invention also includes polynucleotide sequences which can be used as probes for diagnostic reagents, kits (comprising such reagents) and methods which can be used to diagnose or identify the presence or absence of a SARS virus in a biological sample. The invention includes a polynucleotide sequence comprising one or more of the primer sequences identified in Table 32. The invention further includes polynucleotide sequence comprising the complement of one or more of the primer sequences identified in Table 32. The invention provides a SARS polynucleotide sequence SEQ ID NO: 10505. All six reading frames of this sequence are shown in Figure 127 (see also Figure 132). The constituent amino acid sequences from Figure 127, having at least 4 amino acids, are listed as SEQ JD NOS: , 10506 to 10570. The invention includes a polynucleotide sequence comprising SEQ ID NO: 10505. The invention also provides polynucleotide sequences having sequence identity to SEQ ID NO: 10505. The invention also provides for polynucleotide sequences comprising fragments of SEQ JD NO: 10505. In one embodiment, the polynucleotide fragment does not consist entirely of a known SARS virus polynucleotide sequence or of a known coronavirus polynucleotide sequence. The invention includes an amino acid sequence encoded by the polynucleotide sequence of SEQ JD NO: 10505, including the amino acid sequences shown in Figure 127, and particularly those selected from the group consisting of SEQ ID NO s : 10506 to 10570. Preferably, the amino acid sequence comprises SEQ JD NO: 10532 and/or SEQ ID NO: 10533. The invention also provides amino acid sequences having sequence identity to an amino acid sequence encoded by SEQ JD NO: 10505. The invention provides amino acid sequences having sequence identity to an amino acid sequence selected from the group consisting of the sequences shown in Figure 127, and in particular SEQ JD NO s : 10506 to 10570. The invention also provides fragments of amino acid sequences encoded by SEQ JD NO: 10505. The invention also provides fragments of amino acid sequences selected from the group consisting of SEQ ID NO s : 10506 to 10570. In one embodiment, the fragment does not consist entirely of a known amino acid sequence of a SARS virus or a known amino acid sequence of a coronavirus. In one embodiment, the invention includes a polypeptide comprising an amino acid sequence from the 5'3' Frame 3 of Figure 127. Some encoded open reading frames within this translation are: SEQ ID NO: 10533; SEQ JD NO: 10571; SEQ JD NO: 10572; SEQ JD NO: 10573; SEQ ID NO: 10574. The invention includes a polypeptide sequence comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 10533, SEQ ID NO: 10571, SEQ JD NO: 10572, SEQ ID NO: 10573 and SEQ JD NO: 10574. The invention includes a polypeptide having sequence identity to the amino acid sequence selected from the group consisting of SEQ JD NO: 10533, SEQ JD NO: 10571, SEQ JD NO: 10572, SEQ JD NO: 10573 and SEQ JD NO: 10574, The invention includes a fragment of a polypeptide sequence comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 10533, SEQ ID NO: 10571, SEQ JD NO: 10572, SEQ JD NO: 10573 and SEQ ID NO: 10574. Partial BLAST results of SEQ ID NO: 10533 against GenBank are given below: >gi|773960l|gb|AAF68926.l|AF207902_ll nucleocapsid protein [murine hepatitis virus strain ML-11] Length = 451 Score = 147 bits (370), Expect = 3e-34 Identities = 102/252 (40%), Positives = 137/252 (54%), Gaps = 18/252 (7%) Query: 49 SWFTALTQHGK-EELRFPRGQGVPINTNSGPDDQIGYYRRATRR-VRGGDGKMKELSPRW 106 SWF+ +TQ K +E +F +GQGVPI + +Q GY+ R RR + DG+ K+L PRW ) Sbjct: 63 SWFSGITQFQKGKEFQFAQGQGVPIASGIPASEQKGYWYRHNRRSFKTPDGQHKQLLPRW 122 Query: 107 YFYYLGTGPEASLPYGANKΞGIVWVATEGALNTPKDHIGTRNPNNNAATVLQLPQGTTLP 166 YFYYLGTGP A YG + EG+VWVA++ A + R+P+++ A + GT LP Sbjct: 123 YFYYLGTGPHAGAEYGDDIEGWWVASQQADTKTTADWΞRDPSSHEAIPTRFAPGTVLP 182 Query: 167 KGFYAEGSRGGSQASSRSSSRSRGNSRNSTPGSSRGNSPARMASGGGETALALLLLDRLN 226 +GFY EGS + AS S N SS PA +A L+L +L Sbjct: 183 QGFYVEGSGRSAPASRSGSRSQSRGPNNRARSSSNQRQPASAVKPDMAEEIAALVLAKLG 242 Query: 227 QLESKVSGKGQQQQGQTVTKKSAAEASK KPRQKRTATKQYNVTQAFGRRGPEQTQG 282 + GQ +Q VTK+SA Ξ + KPRQKRT KQ V Q FG+RGP Q Sbjct: 243 K DAGQPKQ VTKQSAKEVRQKILTKPRQKRTPNKQCPVQQCFGKRGPNQ 290 Query: 283 NFGDQDLIRQGT 294 NFG ++++ GT Sbjct: 291 NFGGSEMLKLGT 302 >gi 13132999 |gb|AAC16422.l| nucleocapsid protein [murine hepatitis virus strain 2] Length = 451 Score = 147 bits (370) , Expect = 3e-34 Identities = 102/252 (40%), Positives = 137/252 (54%), Gaps = 18/252 (7%) Query: 49 SWFTALTQHGK-EELRFPRGQGVPINTNSGPDDQIGYYRRATRR-VRGGDGKMKELSPRW 106 SWF+ +TQ K +E +F +GQGVPI + +Q GY+ R RR + DG+ K+L PRW Sbjct: 63 SWFSGITQFQKGKEFQFAQGQGVPIASGIPASEQKGYWYRHNRRSFKTPDGQHKQLLPRW 122 Query: 107 YFYYLGTGPEASLPYGANKEGIVWVATEGALNTPKDHIGTRNPNNNAATVLQLPQGTTLP 166 YFYYLGTGP A YG + EG+VWVA++ A + R+P+++ A + GT LP Sbjct: 123 YFYYLGTGPHAGAEYGDDIEGWWVASQQADTKTTADWERDPSSHEAIPTKFAPGTVLP 182 Query: 167 KGFYAEGSRGGSQASSRSSSRSRGNSRNSTPGSSRGNSPARMASGGGΞTALALLLLDRLN 226 +GFY EGS + AS S N SS PA +A L+L +L Sbjct: 183 QGFYVEGSGKSAPASRSGSRSQSRGPNNRARSSSNQRQPASAVKPDMAEEIAALVLAKLG 242 Query: 227 QLESKVSGKGQQQQGQTVTKKSAAEASK KPRQKRTATKQYNVTQAFGRRGPEQTQG 282 + GQ +Q VTK+SA E + KPRQKRT KQ V Q FG+RGP Q Sbjct: 243 K DAGQPKQ VTKQSAKEVRQKILTKPRQKRTPNKQCPVQQCFGKRGPNQ 290 Query: 283 NFGDQDLIRQGT 294 NFG ++++ GT Sbjct: 291 NFGGSEMLKLGT 302 >gi|127877|sp|P03417 |NCAP_CVMJH Nucleocapsid protein gi j 74859 |pir j I VHIHMJ nucleocapsid protein - murine hepatitis virus (strain JHM) gi I 58973 I emb|CAA25497.11 nucleocapsid protein [Murine hepatitis virus] Length = 455 Score = 146 bits (369), Expect = 4e-34 Identities = 110/254 (43%), Positives = 142/254 (55%), Gaps = 22/254 (8%) Query: 49 SWFTALTQHGK-EELRFPRGQGVPINTNSGPDDQIGYYRRATRR-VRGGDGKMKΞLSPRW 106 SWF+ +TQ K +E +F +GQGVPI Q GY+ R RR + DG+ K+L PRW Sbjct: 67 SWFSGITQFQKGKΞFQFAQGQGVPIANGIPASQQKGYWYRHNRRSFKTPDGQQKQLLPRW 126 Query: 107 YFYYLGTGPEASLPYGANKEGIVWVATEGALNTPKDHIGTRNPNNNAATVLQLPQGTTLP 166 YFYYLGTGP A YG + EG+VWVA++ A I R+P+++ A + GT LP Sbjct: 127 YFYYLGTGPYAGAEYGDDIEGWWVASQQAETRTSADIVERDPSSHEAIPTRFAPGTVLP 186 Query: 167 KGFYAEGSRGGSQASSRSSSR—SRGNSRNSTPGSSRGNSPARMASGGGETALALLLLDR 224 +GFY EGS G S +SRS SR SRG N SS PA +A L+L + Sbjct: 187 QGFYVEGS-GRSAPASRSGSRPQSRG-PNNRARSSSNQRQPASTVKPDMAEEIAALVLAK 244 Query: 225 LNQLESKVSGKGQQQQGQTVTKKSAAEASK KPRQKRTATKQYNVTQAFGRRGPEQT 280 L + GQ +Q VTK+SA E + KPRQKRT KQ V Q FG+RGP Q Sbjct: 245 LGK DAGQPKQ VTKQSAKEVRQKILNKPRQKRTPNKQCPVQQCFGKRGPNQ- 294 Query: 281 QGNFGDQDLIRQGT 294 NFG ++++ GT Sbjct: 295 --NFGGPEMLKLGT 306 >gi|6625766|gb|AAFl9389.1|AF201929_7 nucleocapsid protein [murine hepatitis virus strain 2] gi|7769348|gb|AAF69338.l|AF208066_ll nucleocapsid protein [murine hepatitis virus] Length = 451 Score = 146 bits (368) , Expect = 5e-34 Identities = 102/252 (40%), Positives = 137/252 (54%), Gaps = 18/252 (7%) Query: 49 SWFTALTQHGK-EELRFPRGQGVPINTNSGPDDQIGYYRRATRR-VRGGDGKMKELSPRW 106 SWF+ +TQ K +E +F +GQGVPI + +Q GY+ R RR + DG+ K+L PRW Sbjct: 63 SWFSGITQFQKGKEFQFAQGQGVPIASGIPASEQKGYWYRHNRRSFKTPDGQHKQLLPRW 122 Query: 107 YFYYLGTGPEASLPYGANKΞGIVWVATEGALNTPKDHIGTRNPNNNAATVLQLPQGTTLP 166 YFYYLGTGP A YG + EG+VWVA++ A + R+P+++ A + GT LP Sbjct: 123 YFYYLGTGPHAGAEYGDDIEGWWVASQQADTKTTADWERDPSSHEAIPTRFAPGTVLP 182 Query: 167 KGFYAΞGSRGGSQASSRSSSRSRGNSRNSTPGSSRGNSPARMASGGGΞTALALLLLDRLN 226 +GFY EGS + AS S N SS PA +A L+L +L Sbjct: 183 QGFYVΞGSGRSAPASRSGSRSQSRGPNNRARSSSNQRQPASAVKPDMΑEEIAALVLAKLG 242 Query: 227 QLESKVSGKGQQQQGQTVTKKSAAEASK KPRQKRTATKQYNVTQAFGRRGPEQTQG 282 + GQ +Q VTK+SA E + KPRQKRT KQ V Q FG+RGP Q Sbjct: 243 K DAGQPKQ VTKQSAKEVRQKILTKPRQKRTPNKQCPVQQCFGKRGPNQ 290 Query: 283 NFGDQDLIRQGT 294 NFG ++++ GT Sbjct: 291 NFGGSEMLKLGT 302 >gi|21734854|gb|AAM77005.l|AF481863_7 phosphorylated nucleocapsid protein N [porcine hemagglutinating encephalomyelitis virus] Length = 449 Score = 145 bits (366) , Expect = 8e-34 Identities = 107/253 (42%), Positives = 145/253 (57%), Gaps = 18/253 (7%) Query: 49 SWFTALTQHGK-EELRFPRGQGVPINTNSGPDDQIGYYRRATRR-VRGGDGKMKELSPRW 106 SWF+ +TQ K +E F GQGVPI + GY+ R RR + DG ++L PRW Sbjct: 64 SWFSGITQFQKGKEFEFAEGQGVPIAPGVPATEAKGYWYRHNRRSFKTADGNQRQLLPRW 123 Query: 107 YFYYLGTGPEASLPYGANKEGIVWVATEGA-LNTPKDHIGTRNPNNNAATVLQLPQGTTL 165 YFYYLGTGP A YG + +G+ WVA+ A +NTP D I R+P+++ A + P GT L Sbjct: 124 YFYYLGTGPHAKHQYGTDIDGVFWVASNQADINTPAD-IVDRDPSSDEAIPTRFPPGTVL 182 Query: 166 PKGFYAEGSRGGSQASSRSSSRSRGNSRNSTPGSSRGNSPARMASGGGETALALLLLDRL 225 P+G+Y EGS G S +SRS+SR+ N S SR NS R ++ G +A D++ Sbjct: 183 PQGYYIEGS-GRSAPNSRSTSRA-PNRAPSAGSRSRANSGNRTSTPGVTPDMA DQI 236 Query: 226 NQLESKVSGKGQQQQGQTVTKKSAAEASK KPRQKRTATKQYNVTQAFGRRGPEQTQ 281 L GK + Q VTK++A E + KPRQKR+ KQ V Q FG+RGP Q Sbjct: 237 ASLVLAKLGK-DATKPQQVTKQTAKEVRQKILNKPRQKRSPNKQCTVQQCFGKRGPNQ-- 293 Query: 282 GNFGDQDLIRQGT 294 NFG ++++ GT . Sbjct: 294 -NFGGGEMLKLGT 305 >gi 1232957651 gb|AAL80036.11 nucleocapsid protein [porcine hemagglutinating encephalomyelitis virus] Length = 449 Score = 145 bits (365), Expect = le-33 Identities = 107/253 (42%), Positives = 145/253 (57%), Gaps = 18/253 (7%) Query: 49 SWFTALTQHGK-EELRFPRGQGVPINTNSGPDDQIGYYRRATRR-VRGGDGKMKELSPRW 106 SWF+ +TQ K +E F GQGVPI + GY+ R RR + DG ++L PRW Sbjct: 64 SWFSGITQFQKGKEFEFAΞGQGVPIAPGVPSTEAKGYWYRHNRRSFKTADGNQRQLLPRW 123 Query: 107 YFYYLGTGPEASLPYGANKEGIVWVATEGA-LNTPKDHIGTRNPNNNAATVLQLPQGTTL 165 YFYYLGTGP A YG + +G+ WVA+ A +NTP D I R+P+++ A + P GT L Sbjct: 124 YFYYLGTGPHAKDQYGTDIDGVFWVASNQADINTPAD-IVDRDPSSDΞAIPTRFPPGTVL 182 Query: 166 PKGFYAEGSRGGSQASSRSSSRSRGNSRNSTPGSSRGNSPARMASGGGETALALLLLDRL 225 P+G+Y EGS G S +SRS+SR+ N S SR NS ' R ++ G +A D++ Sbjct: 183 PQGYYIEGS-GRSAPNSRSTSRA-PNRAPSAGSRSRANSGNRTSTPGVTPDMA DQI 236 Query: 226 NQLESKVSGKGQQQQGQTVTKKSAAΞASK KPRQKRTATKQYNVTQAFGRRGPEQTQ 281 L GK + Q VTK++A Ξ + KPRQKR+ KQ V Q FG+RGP Q Sbjct: 237 ASLVLAKLGK-DATKPQQVTKQTAKΞVRQKILNKPRQKRSPNKQCTVQQCFGKRGPNQ— 293 Query: 282 GNFGDQDLIRQGT 294 NFG ++++ GT ■ Sbjct: 294 -NFGGGΞMLKLGT 305 These results indicate that SEQ ID NO: 10533 has functional similarities to a coronavirus nucleocapsid protein. In one embodiment, the invention comprises an amino acid sequence from the 5'3' Frame 1 of Figure 127 e.g. SEQ JD NO s : 10506-10514. Some encoded open reading frames within this region are SEQ JD NO s : 10575 to 10578. Accordingly, the invention includes a polypeptide comprising the amino acid sequence selected from the group consisting of SEQ ID NO: 10575, SEQ ID NO: 10576, SEQ JD NO: 10577 and SEQ JD NO: 10578. The invention includes a polypeptide comprising an amino acid sequence having sequence identity to a sequence selected from the group consisting of SEQ JD NO: 10097, SEQ ID NO: 10576, SEQ JD NO: 10577 and SEQ JD NO: 10578. The invention includes a fragment of a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 10097, SEQ JD NO: 10576, SEQ JD NO: 10577 and SEQ JD NO: 10578. In one embodiment, the invention includes a polypeptide comprising an amino acid sequence from the 3'5' Frame 2 of Figure 127 e.g. SEQ JD NO s : 10547-10559. An open reading frame within this region is SEQ ID NO: 10579. The invention includes a polypeptide comprising an amino acid sequence of SEQ ID NO: 10579. The invention includes a polypeptide comprising an amino acid sequence having sequence identity to SEQ JD NO: 10579. The invention includes a fragment of a polypeptide comprising an amino acid sequence of SEQ ID NO: 10579. The invention also includes polynucleotide sequences which can be used as probes for diagnostic reagents, kits (comprising such reagents) and methods which can be used to diagnose or identify the presence or absence of a SARS virus in a biological sample. The invention includes a polynucleotide sequence comprising one or more of the primer sequences identified in Table 33. The invention further includes polynucleotide sequence comprising the complement of one or more of the primer sequences identified in Table 33. The invention includes a polynucleotide sequence comprising SEQ JD NO: 11323. A polypeptide encoded by SEQ ID NO: 11323 is SEQ JD NO: 11324. The invention includes a polypeptide comprising SEQ ID NO: 11324, sequence having sequence identity to SEQ ID NO: 11324 and fragments of SEQ JD NO: 11324. The invention includes a fragment of SEQ JD NO: 11324, wherein said polypeptide fragment begins with a Methionine. Accordingly, the invention includes a polynucleotide sequence comprising SEQ JD NO: 11323. It also provides polynucleotide sequences having sequence identity to SEQ ID NO: 11323. The invention also provides for polynucleotide sequences comprising fragments of SEQ JD NO: 11323. In one embodiment, the polynucleotide fragment does not consist entirely of a known SARS polynucleotide sequence or a known coronavirus polynucleotide sequence. The invention includes an amino acid sequence encoded by the polynucleotide sequence SEQ JD NO: 11323, including the amino acid sequence of SEQ ID NO: 11324. The invention also provides amino acid sequences having sequence identity to an amino acid sequence encoded by SEQ ID NO: 11323. The invention provides amino acid sequences having sequence identity to SEQ ID NO: 11324. The invention provides fragments of amino acid sequences encoded by SEQ JD NO: 11323. The invention also provides fragments of amino acid sequences of SEQ ID NO: 11324. In one embodiment, the fragment does not consist entirely of a known SARS amino acid sequence or a known coronavirus amino acid sequence. The invention also includes polynucleotide sequences which can be used as probes for diagnostic reagents, kits (comprising such reagents) and methods which can be used to diagnose or identify the presence or absence of a SARS virus in a biological sample. The invention includes a polynucleotide sequence comprising one or more of the primer sequences identified as SEQ ID NO s : 11325-11440 (left part) and SEQ ID NO s : 11441-11551 (right part). The invention further includes polynucleotide sequence comprising the complement of one or more of the primer sequences identified as SEQ ID NO s : 11325-11551. The invention includes a polypeptide comprising SEQ JD NO: 11552. The SARS virus contains polymorphism at the Isoleucine residue Ile-324. The invention includes a polypeptide comprising an amino acid sequence having sequence identity to SEQ JD NO: 11552, wherein said polypeptide includes an amino acid sequence selected from the group consisting of YSYAI (SEQ ID NO: 11553), SYAIH (SEQ JD NO: 11554), YAIHH (SEQ ID NO: 11555), IHHDK (SEQ JD NO: 11556), SYAI (SEQ JD NO: 11557), YAIH (SEQ JD NO: 11558), AIHH (SEQ JD NO: 11559), IHHD (SEQ JD NO: 11560), YAI, AIH, and IHH. The invention includes a 5 fragment of a polypeptide comprising SEQ JD NO: 11552, wherein said fragment includes an amino acid sequence selected from the group consisting of YSYAI (SEQ ID NO: 11553), SYAIH (SEQ ID NO: 11554), YAIHH (SEQ ID NO: 11555), IHHDK (SEQ ID NO: 11556), SYAI (SEQ JD NO: 11557), YAIH (SEQ JD NO: 11558), AIHH (SEQ ID NO: 11559), IHHD (SEQ ID NO: 11560), YAI, AIH, and IHH. 0 The invention includes a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 11561 and SEQ JD NO: 11562. The invention includes a fragment of a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 11561 and SEQ JD NO: 11562. The invention includes a diagnostic kit comprising a polypeptide comprising at least one of L5 the amino acid sequences selected from the group consisting of SEQ JD NO s : 11561 and 11562. The invention includes a diagnostic kit comprising a polynucleotide sequence encoding a polypeptide comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NO s : 11561 and 11562. The invention includes an immunogenic composition composing a polypeptide comprising at least one of the amino acid sequences ',0 selected from the group consisting of SEQ ID NO s : 11561 and 11562. The invention includes an antibody which recognizes a polypeptide comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NO s : 11561 and 11562. The invention includes a polynucleotide sequence SEQ JD NO: 11563 or a fragment thereof or a sequence having sequence identity thereto. Polypeptide sequences which can be 5 translated from SEQ ID NO: 11563 are shown in Figure 128. The constituent amino acid sequences from Figure 128, having at least 4 amino acids, are listed as SEQ JD NO s : 11564 to 11617. The invention includes a polypeptide sequence selected from the group consisting of the sequences of Figure 128, or a fragment thereof or a sequence having sequence identity thereto 3 e.g. SEQ JD NO s : 11563 to 11617. A polypeptide sequence within SEQ JD NO: 11600 is SEQ JD NO: 11618. The invention includes a polypeptide comprising SEQ JD NO: 11618, or a fragment thereof or a sequence having sequence identity thereto. A polypeptide sequence within SEQ ID NO: 11602 is SEQ ID NO: 11641. The invention includes a polypeptide comprising SEQ JD NO: 11641, or a fragment thereof or a sequence having sequence identity thereto. A polypeptide sequence within SEQ ID NO: 11609 is SEQ JD NO: 11619. The invention includes a polynucleotide encoding (i) an amino acid sequence selected from the group consisting of: (1) the amino acid sequences of Figure 128, and in particular SEQ JD NO s : 11564-11617; (2) SEQ JD NO: 11618; and (3) SEQ ID NO: 11619, or (ii) a fragment thereof. The invention includes a diagnostic kit comprising a one or more of these proteins. The invention includes a diagnostic kit comprising a polynucleotide sequence encoding one or more of these polypeptide sequences. The invention includes an antibody which recognizes one or more of the polypeptide sequences. The SARS viras may contain polymorphism at isoleucine residue Ile-326 in SEQ ID NO: 11620 (Chi-PEP3). The invention includes a polypeptide comprising an amino acid sequence having sequence identity to SEQ ID NO: 11620, wherein said polypeptide includes an amino acid sequence selected from the group consisting of YAIHH (SEQ ID NO: 11621) and YATHH (SEQ ID NO: 11622). The invention includes a fragment of a polypeptide comprising SEQ JD NO: 11620, wherein said fragment includes an amino acid sequence selected from the group consisting of YAIHH (SEQ ID NO: 11621) and YATHH (SEQ ID NO: 11622). The SARS viras may contain polymorphism at glutamine residue Gln-830 in SEQ ID NO: 11620. The invention includes a polypeptide comprising an amino acid sequence having sequence identity to SEQ ID NO: 11620, wherein said polypeptide includes an amino acid sequence selected from the group consisting of ASQAW (SEQ JD NO: 11623) and ASRAW (SEQ ID NO: 11624). The invention includes a fragment of a polypeptide comprising SEQ JD NO: 11620, wherein said fragment includes an amino acid sequence selected from the group consisting of ASQAW (SEQ JD NO: 11623) and ASRAW (SEQ JD NO: 11624). The SARS viras may contain polymorphism at aspartic acid residue Asp-935 in SEQ JD NO: 11620. The invention includes a polypeptide comprising an amino acid sequence having sequence identity to SEQ ID NO: 11620, wherein said polypeptide includes an amino acid sequence selected from the group consisting of DADST (SEQ ID NO: 11625) and DAYST (SEQ JD NO: 11626). The invention includes a fragment of a polypeptide comprising SEQ JD NO: 11620, wherein said fragment includes an amino acid sequence selected from the group consisting of DADST (SEQ ID NO: 11625) and DAYST (SEQ JD NO: 11626). The SARS viras may contain polymorphism at serine residue Ser-577 in SEQ ID NO: 11627 (Chi-PEP4). The invention includes a polypeptide comprising an amino acid sequence having sequence identity to SEQ ID NO: 11627, wherein said polypeptide includes an amino acid sequence selected from the group consisting of PCSFG (SEQ ID NO: 11628) and PCAFG (SEQ JD NO: 11629). The invention includes a fragment of a polypeptide comprising SEQ ID . NO: 11627, wherein said fragment includes an amino acid sequence selected from the group consisting of PCSFG (SEQ ID NO: 11628) and PCAFG (SEQ JD NO: 11629). The SARS virus may contain polymorphism at valine residue Nal-68 in SEQ JD NO: 11630 (Chi-PEP8). The invention includes a polypeptide comprising an amino acid sequence having sequence identity to SEQ JD NO: 11630, wherein said polypeptide includes an amino acid sequence selected from the group consisting of LAWY (SEQ JD NO: 11631) and LAAVY (SEQ JD NO: 11632). The invention includes a fragment of a polypeptide comprising SEQ JD NO: 11630, wherein said fragment includes an amino acid sequence selected from the group consisting of LAWY (SEQ JD NO: 11631) and LAAVY (SEQ JD NO: 11632). The SARS viras may contain polymorphism at isoleucine residue fie-50 in SEQ JD NO: 11633 (Chi-PEP13). The invention includes a polypeptide comprising an amino acid sequence having sequence identity to SEQ JD NO: 11633, wherein said polypeptide includes an amino acid sequence selected from the group consisting of NN AS (SEQ JD NO: 11634) and NNTAS (SEQ JD NO: 11635). The invention includes a fragment of a polypeptide comprising SEQ JD NO: 11633, wherein said fragment includes an amino acid sequence selected from the group consisting of NN AS (SEQ JD NO: 11634) and NNTAS (SEQ JD NO: 11635). The SARS virus may contain a polymorphism at Serine residue Ser-943 in SEQ ID NO: 11636. The invention includes a polypeptide comprising an amino acid sequence having sequence identity to SEQ ID NO: 11636, wherein said polypeptide includes an amino acid sequence selected from the group consisting of AVSAC (SEQ ID NO: 11637) and AVGAC (SEQ JD NO: 11638). The invention includes a fragment of a polypeptide comprising SEQ JD NO: 11636, wherein said fragment includes an amino acid seuence selected from the group consisting of AVSAC (SEQ JD NO: 11637) and AVGAC (SEQ ID NO: 11638). The invention includes a polynucleotide SEQ JD NO: 11639, or a fragment thereof or a sequence having sequence identity thereto. The invention includes a polypeptide encoded by the polynucleotide sequence set forth in SEQ JD NO: 11639, or a fragment thereof or a polypeptide sequence having sequence identity thereto. The invention includes a polynucleotide set forth in SEQ JD NO: 11640, or a fragment thereof or a sequence having sequence identity thereto. The invention includes a polypeptide encoded by the polynucleotide sequence set forth in SEQ JD NO: 11640, or a fragment thereof or a polypeptide sequence having sequence identity thereto. The invention includes each of the polynucleotides identified above. The invention includes each of the polynucleotides set forth in the sequence listing. The invention further includes polynucleotides having sequence identity to each of the polynucleotides identified above. The degree of sequence identity is preferably greater than 50% (e.g., 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more). The invention includes polynucleotide sequences comprising fragments of each of the polynucleotide sequences identified above. The fragments should comprise at least n consecutive polynucleotides from a particular SEQ JD NO:, and, depending on the sequence, n is 7 or more (e.g., 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 45, 50, 55, 60, 65, 70, 80, 90, 100, 120, 130, 140, 150, 160, 170, 180, 190, 200, 210, 220, 230, 240, 250, 260, 270, 280, 290, 300 or more). The invention includes each of the amino acid sequences encoded by each of the polynucleotide sequences identified above. The invention includes each of the amino acid sequences encoded by each of the polynucleotide sequences set forth in the sequence listing. The invention fμrther includes amino acid sequences having sequence identity to the amino acid sequences encoded by each of the polynucleotide sequences identified above. The degree of sequence identity is preferably greater than 50% (e.g., 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more). The invention further includes fragments of amino acid sequences encoded by each of the polynucleotide sequences identified above. The fragments should comprise at least n consecutive amino acids from a particular SEQ JD NO:, and, depending on the sequence, n is 7 or more (e.g., 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 45, 50, 55, 60, 65, 70, 80, 90, 100, 120, 130, 140, 150, 160, 170, 180, 190, 200, 210, 220, 230, 240, 250, 260, 270, 280, 290, 300 or more). The invention includes each of the amino acid sequences identified above. The invention includes each of the amino acid sequence set forth in the sequence listing. The invention further includes amino acid sequences having sequence identity to each of the amino acid sequences identified above. The degree of sequence identity is preferably greater than 50% (e.g., 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%), 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more). The invention further includes fragments of the amino acid sequences identified above. The fragments should comprise at least n consecutive amino acids from a particular SEQ ID NO:, and, depending on the sequence, n is 7 or more (e.g., 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 45, 50, 55, 60, 65, 70, 80, 90, 100, 120, 130, 140, 150, 160, 170, 180, 190, 200, 210, 220, 230, 240, 250, 260, 270, 280, 290, 300 or more). The invention includes polynucleotides encoding each of the amino acid sequences identified above. The invention includes polynucleotides encoding each of the amino acid sequences set forth in the sequence listing. The invention further includes polynucleotides having sequence identity with each of the polynucleotides encoding each of the amino acid sequences identified above. The degree of sequence identity is preferably greater than 50% (e.g., 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more). The invention further includes fragments of polynucleotides encoding each of the amino acid sequences identified above. The fragments should comprise at least n consecutive polynucleotides from a particular SEQ ID NO:, and, depending on the sequence, n is 7 or more (e.g., 7, 8, 9, 10, 11, 12, 13, 14, 15, 1.6,J7, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 45, 50, 55, 60, 65, 70, 80, 90, 100, 120, 130, 140, 150, 160, 170, 180, 190, 200, 210, 220, 230, 240, 250, 260, 270, 280, 290, 300 or more). As described in more detail below, polynucleotides for use as primers and/or as probes may contain at least 4 or 8 contiguous nucleotides from a polynucleotide sequence of the invention e.g. at least 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, or 30 contiguous nucleotides and up to about 50, 75, 100, 200 contiguous nucleotides or more. While 6-8 nucleotides may be a workable length, sequences of 10-12 nucleotides are preferred, and about 13, 14, 15, 16, 17, 18, 19, 20, or 21 or more nucleotides or more appears optimal for hybridisation. In one embodiment, the invention is directed to polynucleotides and amino acid sequences that do not consist entirely of a known SARS virus polynucleotide or amino acid sequence or of a known coronavirus polynucleotide or amino acid sequence. In one embodiment, the polynucleotides and amino acid sequences of the invention do not consist entirely of the sequence SEQ ID NO: 1. In another embodiment, the polynucleotides and amino acid sequences of the invention do not consist entirely of the sequence SEQ JD NO: 2. SEQ ID NO: 9967 is a SARS genome sequence of the Frankfurt (FRA) isolate (GenBank: AY310120). Compared to SEQ ID NO: 1, it differs at nucleotides 2546, 2590, 11437, 18954, 19073, 20585, 20899, 23209, 24922, 26589 & 28257; compared to SEQ ID NO:2, it differs at nucleotides 2560, 7922, 11451, 16625, 18968 & 19067. Further genome sequences have become available from GenBank, since this application was originally filed, under accession numbers including AY559097, AY559096, AY559095, AY559094, AY559093, AY559092, AY559091, AY559090, AY559089, AY559088, AY559087, AY559086, AY559085, AY559084, AY559083, AY559082, AY559081, AY274119, AY323977, AY291315, AY502932, AY502931, AY502930, AY502929, AY502928, AY502927, AY502926, AY502925, AY502924, AY502923, AY291451, AY390556, AY395003, AY395002, AY395001, AY395000, AY394999, AY394998, AY394997, AY394996, AY394995, AY394994, AY394993, AY394992, AY394991, AY394990, AY394989, AY394987, AY394986, AY394985, AY394983, AY394979, AY394978, AY508724, AY394850, AY463059, AY463060, AY313906, AY310120, AY461660, AY485278, AY485277, AY345988, AY345987, AY345986, AY282752, AY357076, AY357075, AY350750, AY304495, AY304488, AY304486, AY427439, AY283798, AY278491, AY278489, AY362699, AY362698, AY283797, AY283796, AY283795, AY283794, AY278741, AY351680, AP006561, AP006560, AP006559, AP006558, AP006557, AY278554, AY348314, AY338175, AY338174, AY321118, AY279354, AY278490, AY278487, AY297028, AY278488, andNC_004718. In another embodiment, the invention is directed to polynucleotides that encode proteins which are not immunologically cross reactive with a protein of a mouse hepatitis virus, a bovine coronavirus or an avian infectious bronchitis viras. In another embodiment, the invention is directed to proteins which are not immunologically cross reactive with a protein of a mouse hepatitis virus, a bovine coronavirus or an avian infectious bronchitis virus. Each of the polynucleotides identified above may be used to encode a portion of a fusion protein. Accordingly, the invention complies one or more of the polynucleotides identified above wherein the polynucleotides encoding for the start codon are removed. The invention further comprises one or more of the amino acids identified above wherein the starting methionine is removed. Any of the polynucleotide or amino acid sequences discussed above may be used in vaccines for the treatment or prevention of SARS virus infection, including as a SARS viral antigen. Additionally, any of the polynucleotides or amino acid sequences discussed above may be used as diagnostic reagents, or in kits (comprising such reagents) or in methods used to diagnose or identify the presence or absence of a SARS virus in a biological sample. SARS viral antigens of the invention may include a polypeptide with 99%, 95%, 90%, 85%, or 80% homology to one or more of the group consisting of the following proteins: nonstructural protein 2 (NS2); hemagglutinin-esterase glycoprotein (HE) (also refeoed to as E3), spike glycoprotein (S) (also refeoed to as E2), nonstructural region 4 (NS4), envelope (small membrane) protein (E) (also referred to as sM), membrane glycoprotein (M) (also referred to as El), nucleocapsid phosphoprotein (N) or RNA dependent RNA polymerase (pol). A detailed discussion of Coroaviras biology can be found in Fields Virology (2nd ed), Fields et al. (eds.), B.N. Raven Press, New York, NY., Chapter 35. Another example of a SARS virus isolate is set forth in Example 1 below. The invention includes each of the polypeptide and polynucleotide sequences identified in Example 1. hi addition, the invention includes vaccine formulations comprising one or more of the polypeptide or polynucleotide sequences identified in Example 1. The invention includes diagnostic regaents, kits (comprising such reagents) and methods which can be used to diagnose or identify the presence or absence of a SARS virus in a biological sample using one or more of the polypeptide or polynucleotide sequences identified in Example 1. The invention includes methods for the treatment or prevention of SARS viras infection utilizing small molecule viral inhibitors and combinations of small molecule viral inhibitors and kits for the treatment of SARS. The small molecule inhibitors may specifically target one or more of the polypeptides or polynucleotides identified in Example 1. Further discussion of terms used in the application follows below. "Respiratory Virus" as used herein refers to a virus capable of infecting the human respiratory tract. Respiratory Viral Antigens suitable for use in the invention include Severe Acute Respiratory Syndrome viras, coronavirus, influenza viras, human rhinovirus (BORN), parainfluenza virus (PJN), respiratory syncytial viras (RSN), adenovirus, metapneumovirus, and rhinovirus. The terms "polypeptide", "protein" and "amino acid sequence" as used herein generally refer to a polymer of amino acid residues and are not limited to a minimum length of the product. Thus, peptides, oligopeptides,: dimers, mulimers, and the like, are included within the definition. Both full-length proteins and fragments thereof are encompassed by the definition. Minimum fragments of polypeptides useful in the invention can be at least 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or even 15 amino acids. Typically, polypeptides useful in this invention can have a maximum length suitable for the intended application. Generally, the maximum length s not critical and can easily be selected by one skilled in the art. Polypeptides of the invention can be prepared in many ways e.g. by chemical synthesis (at least in part), by digesting longer polypeptides using proteases, by translation from RΝA, by purification from cell culture (e.g. from recombinant expression), from the organism itself (e.g. after viral culture, or direct from patients), from a cell line source etc. A prefeoed method for production of peptides <40 amino acids long involves in vitro chemical synthesis (Bodanszky (1993) Principles of Peptide Synthesis (ISBN: 0387564314); Fields et al. (1997) Methods in Enzymology 289: Solid-Phase Peptide Synthesis. ISBN: 0121821900). Solid-phase peptide synthesis is particularly prefeoed, such as methods based on t-Boc or Fmoc (Chan & White (2000) Fmoc Solid Phase Peptide Synthesis ISBN: 0199637245) chemistry. Enzymatic synthesis (Kullmann (1987) Enzymatic Peptide Synthesis. ISBN: 0849368413) may also be used in part or in full. As an alternative to chemical synthesis, biological synthesis may be used e.g. the polypeptides may be produced by translation. This may be carried out in vitro or in vivo. Biological methods are in general restricted to the production of polypeptides based on L-amino acids, but manipulation of translation machinery (e.g. of aminoacyl tRNA molecules) can be used to allow the introduction of D-amino acids (or of other non natural amino acids, such as iodotyrosine or methylphenylalanine, azidohomoalanine, etc.) (Ibba (1996) Biotechnol Genet Eng Rev 13:197-216.). Where D-amino acids are included, however, it is prefeoed to use chemical synthesis. Polypeptides of the invention may have covalent modifications at the C-terminus and/or N-terminus, particularly where they are for in vivo administration e.g by attachment of acetyl or carboxamide, as in the Fuzeon™ product. Reference to polypeptides and the like also includes derivatives of the amino acid sequences of the invention. Such derivatives can include postexpression modifications of the polypeptide, for example, glycosylation, acetylation, phosphorylation, and the like. Amino acid derivatives can also include modifications to the native sequence, such as deletions, additions and substitutions (generally conservative in nature), so long as the protein maintains the desired activity. These modifications may be deliberate, as through site-directed mutagenesis, or may be accidental, such as through mutations of hosts which produce the proteins or eoors due to PCR amplification. Furthermore, modifications may be made that have one or more of the following effects: reducing toxicity; facilitating cell processing (e.g., secretion, antigen presentation, etc.); and facilitating presentation to B-cells and/or T-cells. "Fragment" or "Portion" as used herein refers to a polypeptide consisting of only a part of the intact full-length polypeptide sequence and structure as found in nature. For instance, a fragment can include a C-terminal deletion and/or an N-terminal deletion of a protein. A "recombinant" protein is a protein which has been prepared by recombinant DNA techniques as described herein. In general, the gene of interest is cloned and then expressed in transformed organisms, as described further below. The host organism expressed the foreign gene to produce the protein under expression conditions. The term "polynucleotide", as known in the art, generally refers to a nucleic acid molecule. A "polynucleotide" can include both double- and single-stranded sequences and refers to, but is not limited to, cDNA from viral, prokaryotic or eukaryotic mRNA, genomic RNA and DNA sequences from viral (e.g. RNA and DNA viruses and retroviruses) or prokaryotic DNA, and especially synthetic DNA sequences. The term also captures sequences that include any of the known base analogs of DNA and RNA, and includes modifications such as deletions, additions and substitutions (generally conservative in nature), to the native sequence, so long as the nucleic acid molecule encodes a therapeutic or antigenic protein. These modifications may be deliberate, as through site-directed mutagenesis, or may be accidental, such as through mutations of hosts that produce the antigens. Modifications of polynucleotides may have any number of effects including, for example, facilitating expression of the polypeptide product in a host cell. Polynucleotides of the invention may be prepared in many ways e.g. by chemical synthesis (e.g. phosphoramidite synthesis of DNA) in whole or in part, by digesting longer nucleic acids using nucleases (e.g. restriction enzymes), by joining shorter nucleic acids or nucleotides (e.g. using ligases or polymerases), from genomic or cDNA libraries, etc. 5 A polynucleotide can encode a biologically active (e.g., immunogenic or therapeutic) protein or polypeptide. Depending on the nature of the polypeptide encoded by the polynucleotide, a polynucleotide can include as little as 10 nucleotides, e.g., where the polynucleotide encodes an antigen. By "isolated" is meant, when referring to a polynucleotide or a polypeptide, that the 0 indicated molecule is separate and discrete from the whole organism with which the molecule is found in nature or, when the polynucleotide or polypeptide is not found in nature, is sufficiently free of other biological macromolecules so that the polynucleotide or polypeptide can be used for its intended purpose. The polynucleotides and polypeptides of the invention are preferably isolated polynucleotides and isolated polypeptides. 5 "Antibody" as known in the art includes one or more biological moieties that, through chemical or physical means, can bind to or associate with an epitope of a polypeptide of interest. The antibodies of the invention include antibodies which specifically bind to a SARS viral antigen. The term "antibody" includes antibodies obtained from both polyclonal and monoclonal preparations, as well as the following: hybrid (chimeric) antibody molecules (see, for example, 10 Winter et al. (1991) Nature 349: 293-299; and US Patent No. 4,816,567; F(ab') 2 and F(ab) fragments; F v molecules (non-covalent heterodimers, see, for example, Inbar et al. (1972) Proc Natl Acad Sci USA 69:2659-2662; and Ehrlich et al. (1980) Biochem 19:4091-4096); single- chain Fv molecules (sFv) (see, for example, Huston et al. (1988) Proc Natl Acad Sci USA 85:5897-5883); dimeric and trimeric antibody fragment constructs; minibodies (see, e.g., Pack >5 et al. (1992) Biochem 31:1579-1584; Cumber et al. (1992) J Immunology 149B: 120-126); humanized antibody molecules (see, for example, Riechmann et al. (1988) Nature 332:323-327; Verhoeyan et al (1988) Science 239:1534-1536; and U.K. Patent Publication No. GB 2,276,169, published 21 September 1994); and, any functional fragments obtained from such molecules, wherein such fragments retain immunological binding properties of the parent antibody i0 molecule. The term "antibody" further includes antibodies obtained through non-conventional processes, such as phage display. As used herein, the term "monoclonal antibody" refers to an antibody composition having a homogeneous antibody population. The term is not limited regarding the species or source of the antibody, nor is it intended to be limited by the manner in which it is made. Thus, the term 5 encompasses antibodies obtained from murine hybridomas, as well as human monoclonal antibodies obtained using human rather than murine hybridomas. See, e.g., Cote, et al Monoclonal Antibodies and Cancer Therapy, Alan R. Liss, 1985, p 77. An "immunogenic composition" as used herein refers to a composition that comprises an antigenic molecule where administration of the composition to a subject results in the development in the subject of a humoral and/or a cellular immune response to the antigenic molecule of interest. The immunogenic composition can be introduced directly into a recipient subject, such as by injection, inhalation, oral, intranasal or any other parenteral, mucosal or fransdermal (e.g., intra-rectally or intra-vaginally) route of administration. The term "derived from" is used to identify the source of molecule (e.g., a molecule can be derived from a polynucleotide, polypeptide, an immortalized cell line can be derived from any tissue, etc.). A first polynucleotide is "derived from" a second polynucleotide if it has the same or substantially the same basepair sequence as a region of the second polynucleotide, its cDNA, complements thereof, or if it displays sequence identity as described above. Thus, a first polynucleotide sequence is "derived from" a second sequence if it has (i) the same or substantially the same sequence as the second sequence or (ii) displays sequence identity to polypeptides of that sequence. A first polypeptide is "derived from" a second polypeptide if it is (i) encoded by a first polynucleotide derived from a second polynucleotide, or (ii) displays sequence identity to the second polypeptides as described above. Thus, a polypeptide (protein) is "derived from" a particular SARS virus if it is (i) encoded by an open reading frame of a polynucleotide of that SARS virus, or (ii) displays sequence identity, as described above, to polypeptides of that SARS viras. Both polynucleotide and polypeptide molecules can be physically derived from a SARS virus or produced recombinantly or synthetically, for example, based on known sequences. A cultured cell or cell line is "derived from" another cell, cells or tissue if it is originally obtained from existing cells or tissue. Non-limiting examples of tissue that cells may be derived from include skin, retina, liver, kidney, heart, brain, muscle, intestinal, ovary, breast, prostate, cancerous tissue, tissue infected with one or more pathogens (e.g., viruses, bacteria etc.) and the like. The cells described herein may also be derived from other cells including, but not limited to, primary cultures, existing immortalized cells line and/or other isolated cells. An "antigen" refers to a molecule containing one or more epitopes (either linear, conformational or both) that will stimulate a host's immune system to make a humoral and/or cellular antigen-specific response. The term is used interchangeably with the term "immunogen." Normally, an epitope will include between about 3-15, generally about 5-15 amino acids. A B-cell epitope is normally about 5 amino acids but can be as small as 3-4 amino acids. A T-cell epitope, such as a CTL epitope, will include at least about 7-9 amino acids, and a helper T-cell epitope at least about 12-20 amino acids. Normally, an epitope will include between about 7 and 15 amino acids, such as, 9, 10, 12 or 15 amino acids. The term "antigen" denotes both subunit antigens, (i.e., antigens which are separate and discrete from a whole organism with which the antigen is associated in nature), as well as, killed, attenuated or 5 inactivated bacteria, viruses, fungi, parasites or other microbes as well as tumor antigens, including extracellular domains of cell surface receptors and intracellular portions that may contain T-cell epitopes. Antibodies such as anti-idiotype antibodies, or fragments thereof, and synthetic peptide mimotopes, which can mimic an antigen or antigenic determinant, are also captured under the definition of antigen as used herein. Similarly, an oligonucleotide or L0 polynucleotide that expresses an antigen or antigenic determinant in vivo, such as in gene therapy and DNA immunization applications, is also included in the definition of antigen herein. An "immunological response" to an antigen or composition is the development in a subject of a humoral and/or a cellular immune response to an antigen present in the composition ■ of interest. For purposes of the present invention, a "humoral immune response" refers to an 5 immune response mediated by antibody molecules, including secretory (IgA) or IgG molecules, while a "cellular immune response" is one mediated by T-lymphocytes and/or other white blood cells. One important aspect of cellular immunity involves an antigen-specific response by cytolytic T-cells ("CTL"s). CTLs have specificity for peptide antigens that are presented in association with proteins encoded by the major histocompatibility complex (MHC) and 0 expressed on the surfaces of cells. CTLs help induce and promote the destruction of intracellular microbes, or the lysis of cells infected with such microbes. Another aspect of cellular immunity involves an antigen-specific response by helper T-cells. Helper T-cells act to help stimulate the function, and focus the activity of, nonspecific effector cells against cells displaying peptide antigens in association with MHC molecules on their surface. A "cellular immune response" 5 also refers to the production of cytokines, chemokines and other such molecules produced by activated T-cells and/or other white blood cells, including those derived from CD4+ and CD8+ T-cells. In addition, a chemokine response may be induced by various white blood or endothelial cells in response to an administered antigen. //. VACCINE FORMULATIONS ) The invention relates to vaccine formulations for the treatment or prevention of Severe Acute Respiratory Syndrome (SARS). Vaccine formulations of the invention include an inactivated (or killed) SARS virus, an attenuated SARS virus, a split SARS virus preparation and a recombinant or purified subunit formulation of one or more SARS viral antigens. The invention includes polypeptides and polynucleotides encoding for SARS viral antigens and immunogenic fragments thereof. Expression and delivery of the polynucleotides of the invention may be facilitated via viral vectors and/or viral particles, including Virus Like Particles (VLPs). A. Inactivated (or Killed) SARS Vaccines The invention includes a composition comprising an inactivated (or killed) SARS virus and methods for the production thereof. Inactivated SARS viral compositions can be used as prophylactic or therapeutic SARS virus vaccine. Preferably the inactivated SARS viras vaccine composition comprises an amount of inactivated SARS virus which, before inactivation, is equivalent to a viras titer of from about 4 to 7 logs plaque forming units (PFU) or 4 to 7 logs tissue culture infectious dose 50 (TCID5 0 ) per milliliter. More preferably, before inactivation the viras titer is from 4 to 11, 7 to 11 or 9 to 11 PFU or TCJD 50 . Still more preferably the inactivated SARS virus vaccine composition comprises an amount of inactivated SARS viras which, before inactivation, is equivalent to a virus titer of from about 5 to 9 PFU or 5 to 9 TCID50 per milliliter. In one embodiment, the PFU or TCJD 50 of the cultured SARS viras at harvest is 6 to 8, more preferably about 7.5 PFU or TCJD 50 per milliliter. Upon concentration of the viral harvest, the PFU or TCJD 50 is preferably 8 to 11, still more preferably about 9 PFU or TCID 50 per milliliter. The vaccine composition comprises a sufficient amount of the SARS virus antigen to produce an immunological response in a primate. Methods of inactivating or killing viruses are known in the art to destroy the ability of the viruses to infect mammalian cells. Such methods include both chemical or physical means. Chemical means for inactivating a SARS virus include treatment of the viras with an effective amount of one or more of the following agents: detergents, formaldehyde, formalin, β- propiolactone, or UV light. Additional chemical means for inactivation include treatment with methylene blue, psoralen, carboxyfullerene (C60) or a combination of any thereof. Other methods of viral inactivation are known in the art, such as for example binary ethylamine, acetyl ethyleneimine, or gamma ioadiation. For example formaldehyde may be used at concentrations such as 0.1 to 0.02%, preferably at 0.02 to 0.1 %, and still more preferably at 0.04 to 0.05%. The inactivating agent is added to virus containing culture supematants prior to or after harvesting said culture supematants from vessels used for virus propagation, either with or without a step of cell disruption for release of cell-associated virus prior to harvesting. Further, the inactivating agent may be added after said culture supematants have been stored frozen and thawed, or after one or more steps of purification to remove cell contaminants. Preferably, however, formaldehyde is added after removal of cells and cellular debris or after one or more purification steps. After addition of formaldehyde, the virus containing mixture is transfeoed into an incubation vessel and incubated at refrigeration temperatures (e.g. +2 to 8°C) or alternatively at elevated temperatures, such as ambient temperatures between approximately 20 and 30°C or at 33°C to 37°C for a period of 12 hours to 7 days, whereby the temperature chosen should be adjusted to the duration of incubation. Prefered conditions are e.g. +2 -8°C for 3-7 days (prefered are 3 -7days), ambient temperatures and incubation for 16 hours to 3 days (prefered 24- 48 hours), or 35-37°C for 12-36 hours. If it is desirable to remove excess formalin, sodium thiosulfate or sodium metabisulfite at 5 equimolar or 1.5 -fold molar concentration (relative to formaldehyde) may be added after completing the inactivation process. For example, β-propiolactone may be used at concentrations such as 0.01 to 0.5%, preferably at 0.5% to 0.2%, and still more preferably at 0.025 to 0.1%. The inactivating agent is added to virus containing culture supematants (virus material) prior to or after harvesting said L0 culture supematants from vessels used for virus propagation, either with or without a step of cell disruption for release of cell-associated virus prior to harvesting. Further, the inactivating agent may be added after said culture supematants have been stored frozen and thawed, or after one or more steps of purification to remove cell contaminants, β-propiolactone is added to the viras material, with the adverse shift in pH to acidity being controlled with sodium hydroxide (e.g., 1 5 N NaOH), a Tris-buffer or sodium bicarbonate solution. After transfering the mixture to another inactivation vessel, the combined inactivating agent- virus materials are incubated at temperatures from 4°C to 37°C, for incubation times of preferably 24 to 72 hours. Another inactivant which may be used is binary ethyleneimine (BEI). Equal volumes of a 0.2 molar bromoethylamine hydrobromide solution and a 0.4 molar sodium hydroxide solution 0 are mixed and incubated at about 37°C. for 60 minutes. The resulting cyclized inactivant is binary ethyleneimine, which is added to the virus materials at 0.5 to 4 percent, and preferably at 1 to 3 percent, volume to volume. The inactivating virus materials are held from about 4°C to 37°C for 24 to 72 hours with periodic agitation. At the end of this incubation 20 ml. of a sterile 1 molar sodium thiosulfate solution was added to insure neutralization of the BEI. 5 In one embodiment, the invention includes an inactivating method is designed to maximize exposure of the virus to the inactivating agent and to minimize long-term exposure of the temperature sensitive SARS viras particles to elevated temperatures. The invention includes an inactivation method comprising exposing the viras to the inactivation agent (such as BPL) for 12 to 24 hours at refrigeration temperatures followed by hydrolysis of any residual inactivating 0 agent by elevating the temperature for only 3 hours. Preferably, the refrigeration temperatures are between 0 and 8°C, more preferably around 4°C. Preferably, the elevated temperature is between 33 and 41°C, more preferably around 37°C. As assessed by a test for residual infectious virus using 10 ml aliquots of the inactivated preparation, the method is able to inactivate SARS- CoV in raw cell culture harvests below a theoretical limit of 0.03 infectious units/ml. 5 Diluted and undiluted samples of the inactivated virus materials are added to susceptible cell (tissue) culture (e.g., VERO) to detect any non-inactivated virus. The cultured cells are passaged multiple times and examined for the presence of SARS virus based on any of a variety of methods, such as, for example, cytopathic effect (CPE) and antigen detection (e.g., via fluorescent antibody conjugates specific for SARS viras). Such tests allow determination of complete virus inactivation. Prior to inactivation, the SARS virus will be cultured in a mammalian cell culture. The cell culture may be adherently growing cells or cells growing in suspension. Preferably the cells are of mammalian origin, but may also be derived from avian (e.g., hens' cells such as hens' embryo cells (CEF cells)), amphibian, reptile, insect, or fish sources. Mammalian sources of cells include, but are not limited to, human or non-human primate (e.g., MRC-5 (ATCC CCL-171), WI-38 (ATCC CCL-75), HeLa cells, human diploid cells, fetal rhesus lung cells (e.g. ATCC CL- 160), human embryonic kidney cells (293 cells, typically transformed by sheared adenovirus type 5 DNA), VERO cells (e.g., from monkey kidneys), horse, cow (e.g., MDBK cells), sheep, dog (e.g., MDCK cells from dog kidneys, ATCC CCL34 MDCK (NBL2) or MDCK 33016, deposit number DSM ACC 2219 as described in WO 97/37001), cat, and rodent (e.g., hamster cells such as BHK21-F, HKCC cells, or Chinese hamster ovary cells (CHO cells)), and may be obtained from a wide variety of developmental stages, including for example, adult, neonatal, fetal, and embryo. In certain embodiments the cells are immortalized (e.g., PERC.6 cells are described, for example, in WO 01/38362 and WO 02/40665, incorporated by reference herein in their entireties, as well as deposited under ECACC deposit number 96022940), or any other cell type immortalized using the techniques described herein. In prefeoed embodiments, mammalian cells are utilized, and may be selected from and/or derived from one or more of the following non-limiting cell types: fibroblast cells (e.g., dermal, lung), endothelial cells (e.g., aortic, coronary, pulmonary, vascular, dermal microvascular, umbilical), hepatocytes, keratinocytes, immune cells (e.g., T cell, B cell, macrophage, NK, dendritic), mammary cells (e.g., epithelial), smooth muscle cells (e.g., vascular, aortic, coronary, arterial, uterine, bronchial, cervical, retinal pericytes), melanocytes, neural cells (e.g., astrocytes), prostate cells (e.g., epithelial, smooth muscle), renal cells (e.g., epithelial, mesangial, proximal tubule), skeletal cells (e.g., chondrocyte, osteoclast, osteoblast), muscle cells (e.g., myoblast, skeletal, smooth, bronchial), liver cells, retinoblasts, and stromal cells. WO 97/37000 and WO 97/37001, incorporated by reference herein in their entireties, describe production of animal cells and cell lines that capable of growth in suspension and in serum free media and are useful in the production and replication of viruses. Preferably, the SARS viruses of the invention are grown on VERO cells or fetal rhesus kidney cells. Culture conditions for the above cell types are well-described in a variety of publications, or alternatively culture medium, supplements, and conditions may be purchased commercially, such as for example, as described in the catalog and additional literature of Cambrex Bioproducts (East Rutherford, NJ). In certain embodiments, the host cells used in the methods described herein are cultured in serum free and/or protein free media. A medium is referred to as a serum-free medium in the context of the present invention in which there are no additives from serum of human or animal origin. Protein-free is understood to mean cultures in which multiplication of the cells occurs with exclusion of proteins, growth factors, other protein additives and non-serum proteins. The cells growing in such cultures naturally contain proteins themselves. Known serum-free media include Iscove's medium, Ultra-CHO medium (BioWhittaker) or EX-CELL (JRH Bioscience). Ordinary serum-containing media include Eagle's Basal Medium (BME) or Minimum Essential Medium (MEM) (Eagle, Science, 130, 432 (1959)) or Dulbecco's Modified Eagle Medium (DMEM or EDM), which are ordinarily used with up to 10% fetal calf serum or similar additives. Optionally, Minimum Essential Medium (MEM) (Eagle, Science, 130, 432 (1959)) or Dulbecco's Modified Eagle Medium (DMEM or EDM) may be used without any seram containing supplement. Protein-free media like PF-CHO (JHR Bioscience), chemically-defined media like ProCHO 4CDM (BioWhittaker) or SMJF 7 (Gibco/BRL Life Technologies) and mitogenic peptides like Primactone, Pepticase or HyPep™ (all from Quest International) or lactalbumin hydrolyzate (Gibco and other manufacturers) are also adequately known in the prior art. The media additives based on plant hydrolyzates have the special advantage that contamination with viruses, mycoplasma or unknown infectious agents can be ruled out. The cell culture conditions to be used for the desired application (temperature, cell density, pH value, etc.) are variable over a very wide range owing to the suitability of the cell line employed according to the invention and can be adapted to the requirements of the SARS viras. The method for propagating the SARS viras in cultured cells (e.g., mammalian cells) includes the steps of inoculating the cultured cells with SARS viras, cultivating the infected cells for a desired time period for virus propagation, such as for example as determined by SARS virus titer or SARS virus antigen expression (e.g., between 24 and 168 hours after inoculation) and collecting the propagated virus. The cultured cells are inoculated with a SARS virus (measured by PFU or TCID 50 ) to cell ratio of 1 : 10000 to 1 : 10. A lower range of ratios may also be used e.g. 1:500 to 1:1, preferably 1:100 to 1:5, more preferably 1:50 to 1:10. The SARS virus is added to a suspension of the cells or is applied to a monolayer of the cells, and the virus is absorbed on the cells for at least 60 minutes but usually less than 300 minutes, preferably between 90 and 240 minutes at 25°C to 40°C, more preferably 28°C to 37°C, still more preferably at about 33 °C. The infected cell culture (e.g., monolayers) may be treated either by freeze-thawing or by enzymatic action to increase the viral content of the harvested culture supematants. The harvested fluids are then either inactivated or stored frozen. A comparison of SARS infected Vero cells grown with and without fetal calf serum ("FCS") is shown in FIGURE 26A. Briefly, Vero cells were split the day before infection and cultivated in T175 flasks. Infection of 90% confluent Vero cell monolayers the following day was performed with a SARS-CoV seed stock (strain FRA, passage 4, Accession number AY310120), with or without 3% FCS (Fig. 26A). The addition of FCS to the cell media showed little impact on viras yield. Cultured cells may be infected at a multiplicity of infection ("m.o.i.") of about 0.0001 to 10, preferably 0.002 to 5, more preferably to 0.001 to 2. Still more preferably, the cells are infected at a m.o.i of about 0.01. A comparison of viral yield at varying m.o.i. levels is shown in FIGURE 26B. Infected cells may be harvested 30 to 60 hours post infection. Preferably, the cells are harvested 34-48 hours post infection. Still more preferably, the cells are harvested 38 to 40 hours post infection. See FIGURE 26C. Methods of purification of inactivated viras are known in the art and may include one or more of, for instance gradient centrifugation, ultracentrifugation, continuous-flow ultracentrifugation and chromatography, such as ion exchange chromatography, size exclusion chromatography, and liquid affinity chromatography. Additional method of purification include ultrafiltration and dialfiltration. See JP Gregersen "Herstellung von Virussimpfstoffen aus Zellkulturen" Chapter 4.2 in Pharmazeutische Biotecnologie (eds. O. Kayser and RH Mueller) Wissenschaftliche Verlagsgesellschaft, Stuttgart, 2000. See also, O'Neil et al, "Virus Harvesting and Affinity Based Liquid Chromatography. A Method for Virus Concentration and Purification", Biotechnology (1993) 11 : 173-177; Prior et al. , "Process Development for Manufacture of Inactivated HJN-1", Pharmaceutical Technology (1995) 30-52; and Majhdi et al, "Isolation and Characterization of a Coronavirus from Elk Calves with diarrhea" Journal of Clinical Microbiology (1995) 35(11): 2937-2942. Other examples of purification methods suitable for use in the invention include polyethylene glycol or ammonium sulface precipitation (see Trepanier et al, "Concentration of human respiratory syncytial viras using ammonium sulfate, polyethylene glycol or hollow fiber ultrafiltration" Journal of Virological Methods (1981) 3(4):201-211; Hagen et al, "Optimization of Poly(ethylene glycol) Precipitation of Hepatitis Viras Used to prepare VAQTA, a Highly Purified Inactivated Vaccine" Biotechnology Progress (1996) 12:406-412; and Carlsson et al, "Purification of Infectious Pancreatic Necrosis Virus by Anion Exchange Chromatography Increases the Specific Infectivity" Journal of Virological Methods (1994) 47:27-36) as well as ultrafiltration and microfiltration (see Pay et al., Developments in Biological Standardization (1985) 60:171-174; Tsurumi et al, "Structure and filtration performances of improved cuprammonium regenerated cellulose hollow fibre (improved BMM hollow fibre) for viras removal" Polymer Journal (1990) 22(12):1085-1100; and Makino et al, "Concentration of live retrovirus with a regenerated cellulose hollow fibre, BMM", Archives of Virology (1994) 139(1- 2):87-96.). Preferably, the viras is purified using chromatography, such as ion exchange chromatography. Chromatic purification allows for the production of large volumes of viras containing suspension. The viral product of interest can interact with the chromatic medium by a simple adsorption desorption mechanism, and large volumes of sample can be processed in a single load. Contaminants which do not have affinity for the adsorbent pass through the column. The virus material can then be eluted in concentrated form. Prefeoed anion exchange resins for use in the invention include DEAE, EMD TMAE. Preferred cation exchange resins may comprise a sulfonic acid-modified surface. In one embodiment, the viras is purified using ion exchange chromatography comprising a strong anion exchange resin (e.g. EMD TMAE) for the first step and EMD-SO 3 (cation exchange resin) for the second step. A metal-binding affinity chromatography step can optionally be included for further purification. (See, e.g., WO 97/06243). A prefeoed resin for use in the invention is Fractogel™ EMD. This synthetic methacrylate based resin has long, linear polymer chains (so-called "tentacles") covalently attached. This "tentacle chemistry" allows for a large amount of sterically accessible ligands for the binding of biomolecules without any steric hindrance. This resin also has improved pressure stability. Column-based liquid affinity chromatography is another preferred purification method for use in the invention. One example of a resin for use in this purification method is Matrex™ Cellufine™ Sulfate (MCS). MCS consists of a rigid spherical (approx. 45-105 μm diameter) cellulose matrix of 3,000 Dalton exclusion limit (its pore structure excludes macromolecules), with a low concentration of sulfate ester functionality on the 6-position of cellulose. As the functional ligand (sulfate ester) is relatively highly dispersed, it presents insufficient cationic charge density to allow for most soluble proteins to adsorb onto the bead surface. Therefore the bulk of the protein found in typical viras pools (cell culture supematants, e.g. pyrogens and most contaminating proteins, as well as nucleic acids and endotoxins) are washed from the column and a degree of purification of the bound viras is achieved. The rigid, high-strength beads of MCS tend to resist compression. The pressure/flow characteristics the MCS resin permit high linear flow rates allowing high-speed processing, even in large columns, making it an easily scalable unit operation. In addition a chromatographic purification step with MCS provides increased assurance of safety and product sterility, avoiding excessive product handling and safety concerns. As endotoxins do not bind to it, the MCS purification step allows a rapid and contaminant free depyrogenation. Gentle binding and elution conditions provide high capacity and product yield. The MCS resin therefore represents a simple, rapid, effective, and cost-saving means for concentration, purification and depyrogenation. In addition, MCS resins can be reused repeatedly. The inactivated viras may be further purified by gradient centrifugation, preferably density gradient centrifugation. For commercial scale operation a continuous flow sucrose gradient centrifugation would be the preferred option. This method is widely used to purify antiviral vaccines and is known to the expert in the field (See JP Gregersen "Herstellung von Virussimpfstoffen aus Zellkulturen" Chapter 4.2 in Pharmazeutische Biotecnologie (eds. O. Kayser and RH Mueller) Wissenschaftliche Verlagsgesellschaft, Stuttgart, 2000.) The density gradient centrifugation step may be performed using laboratory or commercial scale gradient centrifugation equipment. For example, a swinging bucket rotor, a fixed angle rotor, or a vertical tube rotor, particularly for laboratory scale production of the virus. Preferably, the gradient centrifugation step is performed using a swinging bucket rotor. This type of rotor has a sufficiently long pathlength to provide high quality separations, particularly with multicomponent samples. In addition, swinging bucket rotors have greatly reduced wall effects, and the contents do not reorient during acceleration and deceleration. Because of their longer pathlength, separations take longer compared to fixed angle or vertical tube rotors. The prepared sucrose solutions are controlled via refractometer on their sucrose concentration. Sucrose gradients for density gradient centrifugation, such as in a swinging bucket centrifuge tubes may be formed prior to centrifugation by the use of a gradient former (continuous/linear). The volume of sample which can be applied to the gradient in a swinging bucket rotor tube is a function of the cross-sectional area of the gradient that is exposed to the sample. If the sample volume is too high, there is not sufficient radial distance in the centrifuge tube for effective separation of components in a multicomponent sample. An approximate sample volume for swinging bucket rotor SW 28 is 1-5 ml per tube (with a tube diameter of 2.54 cm). The sample is applied to the gradient by pipetting the volume on top of the gradient. The blunt end of the pipette is placed at 45-60° angle to the tube wall, approximately 2-3 mm above the gradient. The sample is injected slowly and allowed to run down the wall of the tube onto the gradient. After centrifugation gradient fractions are recovered by carefully inserting a gauge needle until the bottom of the tube and starting to collect fractions of 2 ml by pumping the liquid from the tube into falcon tubes. Sucrose density gradients suitable for use with this density gradient centrifugation purification step include 0 - 60%, 5 - 60%, 15 - 60%, 0 - 50%, 5 - 50%, 15 - 50%, 0 - 40%, 5 - 40%, and 15 - 40%. Preferably, the sucrose density gradient is 15 - 40%, 5 - 40% or 0 - 40%. -Ill- Alternatively, a discontinuous sucrose density gradient may be used for purification. A discontinuous sucrose density scheme provides for discrete, overlaying layers of differing sucrose concentrations. In one example, a first layer of 50% sucrose is covered by a second layer of 40% sucrose; the second layer is covered by a third layer of 20% sucrose; the third layer is covered by a fourth layer of 10% sucrose; and the fourth layer is covered by the solution containing the viras to be purified. In one embodiment, inactivated virus is purified by a method comprising a first step of chromatography purification and a second step of gradient centrifugation. Preferably the first step comprises liquid affinity chromatography, such as MCS. Preferably, the second step comprises density gradient centrifugation using a swinging bucket rotor. Additional purification methods which may be used to purify inactivated SARS viras include the use of a nucleic acid degrading agent, preferably a nucleic acid degrading enzyme, such as a nuclease having DNase and RNase activity, or an endonuclease, such as from Serratia marcescens, commercially available as Benzonase™, membrane adsorbers with anionic functional groups (e.g. Sartobind™) or additional chromatographic steps with anionic functional groups (e.g. DEAE or TMAE). An ultrafiltration/dialfiltration and final sterile filtration step could also be added to the purification method. Preferably, the purification includes treatment of the SARS viral isolate with one or more nucleic acid degrading enzymes. These enzymes may be used to reduce the level of host cell nucleic acid in the viral purification process. Nucleic acid digesting enzymes for use in cell culture are known in the art and include, for example, Benzonase™. The treatment of the virus with the nucleic acid degrading enzyme and inactivating agent can be performed by a sequential treatment or in a combined or simultaneous manner. Preferably, the nucleic acid degrading agent is added to the virus preparation prior to the addition of the inactivating agent. The purified viral preparation of the invention is substantially free of contaminating proteins derived from the cells or cell culture and preferably comprises less than about 1000, 500, 250, 150, 100, or 50 pg cellular nucleic acid / μg viras antigen, preferably less than about 1000, 500, 250, 150, 100, or 50 pg cellular nucleic acid/ dose. Still more preferably, the purified viral preparation comprises less than about 20 pg, and even more preferably, less than about 10 pg. Methods of measuring host cell nucleic acid levels in a viral sample are known in the art. Standardized methods approved or recommended by regulatory authorities such as the WHO or the FDA are preferred. The invention includes an inactivated vaccine composition comprising a prophylactically effective amount of SARS viral antigen, preferably spike or an immunogenic fragment thereof. The SARS viral antigen is preferably present in a concentration amount of 0.1 to 50 μg antigen/dose, more preferably 0.3 to 30 μg antigen/dose. Still more preferably, the antigen is about 15 μg/dose. In one embodiment, a lower concentration of SARS viral antigen is used in inactivated vaccine compositions of the invention. Such lower concentration vaccines may optionally 5 comprise an adjuvant to boost the host immune response to the antigen. In such a "low dose" vaccine, the SARS viral antigen is preferably present in a concentration of less than 15 μg antigen/dose, (i.e., less than 10, 7.5, 5 or 3 μg antigen/dose. The inactivated vaccine preparations of the invention may further comprise a stabilizer to preserve the integrity of the immunogenic proteins in the inactivated viral preparation. 10 Stabilizers suitable for use in vaccines are known in the art and may include, for example, buffers, sugars, sugar alcohols, and amino acids. Stabilizing buffers are preferably adjusted to a physiological pH range and may include phosphate buffers, Tris buffers, TE (Tris/EDTA), TEN (Tris/NaCl/EDTA) and Earle's salt solution. Stabilizing sugars may include, for example, one or more of saccharose, glucose, fructose, dextranes, dextranesulphate, and trehalose. Stabilizing L5 sugar alcohols may include, for example, Xylite/Xylitole, Mannite/Mannitol, Sorbite/Sorbitol, and Glycerol. Amino acids suitable for use in the invention include, for example, L-glutamine, arginine, cysteine, and lysine. Additional stabilizers which may be used in the invention include Tartaric acid, Pluronic F 68, and Tween 80. SARS viral isolates which may be used for the inactivated viral preparations of the 50 invention may be obtained and identified by any of the mechanisms described supra. For example, a SARS isolate may be obtained from a clinical sample and plaque purified. Such methods of viral isolation are known in the art. Further purification procedures can be applied to ensure the seed virus used for preparation of the vaccine does not contain, for example, unwanted adventitious agents. In one embodiment, :5 viral RNA from the viral isolate can be isolated from the viras, purified (and, optionally, the sequence verified through PCR or other means) and then introduced into a suitable cell culture. As an example of this technique, a clinical viral sample is plaque purified and amplified on vero cells to generate a sufficient amount of the viral sample for analysis. Cellular remnants are then cleared from the supernatant by centrifugation. The viras can then be pelleted by 0 ultracentrifugation and the pellet resuspended in PBS. After further centrifugation purification, the viras containing fraction is treated with a DNase (and optionally also an RNase). Viral RNA is then isolated from this fraction and transfected into a host cell. Examples 2 and 3 provide an illustration of purification of inactivated whole SARS viras using MCS chromatography resin purification followed by density gradient ultracentrifugation. Routes and methods of immunization of the vaccines of the invention are discussed in more detail in a section below. Examples 4 and 5 provide illustrations of a mouse immunization scheme with the inactivated SARS viras of the invention. B. Attenuated SARS Vaccines The invention includes a composition comprising an attenuated SARS virus. This composition can be used as a prophylactic or therapeutic SARS virus vaccine. Methods of attenuating viruses are known in the art. Such methods include serial passage of the SARS viras in cultured cells (e.g., mammalian cell culture, preferably fetal rhesus kidney cells or VERO cells-see the discussion in Section A above regarding culture of SARS viras), until the SARS virus demonstrates attenuated function. The temperature at which the virus is grown can be any temperature at which with tissue culture passage attenuation occurs. Attenuated function of the SARS virus after one or more passages in cell culture can be measured by one skilled in the art. As used herein, attenuation refers to the decreased virulence of the SARS virus in a human subject. Evidence of attenuated function may be indicated by decreased levels of viral replication or by decreased virulence in an animal model. Other methods of producing an attenuated SARS viras include passage of the viras in cell culture at sub-optimal or "cold" temperatures and introduction of attenuating mutations into the SARS viral genome by random mutagenesis (e.g., chemical mutagenesis) or site specific directed mutagenesis. Preparation and generation of attenuated RSV vaccines (the methods of which will generally applicable to SARS virus) are disclosed in, for example, EP 0 640 128, US Patent No. 6,284,254, US Patent No. 5,922,326, US Patent No. 5,882,651. The attenuated derivatives of SARS viras are produced in several ways, such as for example, by introduction of temperature sensitive-mutations either with or without chemical mutagenesis (e.g., 5-fluorouracil), by passage in culture at "cold" temperatures. Such cold adaptation includes passage at temperatures between about 20°C to about 32°C, and preferably between temperatures of about 22°C to about 30°C, and most preferably between temperatures of about 24°C and 28°C. The cold adaptation or attenuation may be performed by passage at increasingly reduced temperatures to introduce additional growth restriction mutations. The number of passages required to obtain safe, immunizing attenuated viras is dependent at least in part on the conditions employed. Periodic testing of the SARS viras culture for virulence and immunizing ability in animals (e.g., mouse, primate) can readily determine the parameters for a particular combination of tissue culture and temperature. The attenuated vaccine will typically be formulated in a dose of from about 10 3 to 10 6 PFU or TCJD 50 , or more for maximal efficacy. Attenuated viras vaccines for SARS-CoV also are produced by creating virus chimeras composing sequences derived from at least two different coronaviruses, one of which is a SARS- CoV. For example, a virus chimera is produced that comprises nonstructural protein encoding genes derived from a first coronavirus (e.g., murine, bovine, porcine, canine, feline, avian coronavirus) and one or more structural protein encoding genes (e.g., spike, E, M) from a SARS- CoV. Alternatively, the viras chimera may comprise sequences derived from a human coronavirus that is not a SARS-CoV (e.g., OC43, 229E) together with sequences from a SARS- 5 CoV. Chimeric coronaviruses of the present invention are generated by a variety of methods, including for example allowing for natural RNA recombination in a eukaryotic (e.g., mammalian) cell that contains RNA from each of the parental coronaviruses (e.g., following infection) or by using standard molecular biology techniques known to those of skill in the art to engineer desired virus chimeras (or portions thereof) as cDNA clones, which may then be used to 0 produce infectious viras (see for example, US 6593111 B2; Yount et al. , 2003, Proc. Natl. Acad. Sci. USA 100(22): 12995-13000). An attenuated phenotype of the coronavirus chimeras described herein can be readily measured by one of skill in the art. Attenuated viruses can be also generated by deleting one or more open reading frames (ORFs) that are not essential for viral replication. Preferably, these deletions occur in the .5 stractural region of the genome, such as ORF 3a, 3b, 6, 7a, 7b, 8a, 8b, 9b. See e.g., Haijema BJ, . Volders H, Rottier PL J Virol. (2004) 78(8):3863-71; and de Haan, C. A., P. S. Masters, X. Shen, S. Weiss, and P. J. Rottier, "The group-specific murine coronavirus genes are not essential, but their deletion, by reverse genetics, is attenuating in the natural host." Virology (2002) 296:177- 189. Deletion of such regions within a coronavirus such as SARS can be achieved, for example, ;0 by reverse genetics or "targeted recombination" (See, e.g., Masters, P. S., "Reverse genetics of the largest RNA viruses", Adv. Virus Res. (1999) 53:245-264. Methods of purification of attenuated virus are known in the art and may include one or more of, for instance gradient centrifugation and chromatography. See Gregersen "Herstellung von Virussimpfstoffen aus Zellkulturen" Chapter 4.2 in Pharmazeutische Biotecnologie (eds. O. 5 Kayser and RH Mueller) Wissenschaftliche Verlagsgesellschaft, Stuttgart, 2000. C. Sylit SARS Vaccines The invention includes a composition comprising a split SARS virus formulation and methods for the manufacture thereof. This composition can be used as a prophylactic or therapeutic SARS virus vaccine. 0 Methods of splitting enveloped viruses are known in the art. Methods of splitting enveloped viruses are disclosed, for example, in WO 02/28422, incorporated herein by reference in its entirety, and specifically including the splitting agents and methods described therein. Methods of splitting influenza viruses are disclosed, for example, in WO 02/067983, WO 02/074336, and WO 01/21151, each of which is incorporated herein by reference in its entirety. 5 The splitting of the virus is carried out by disrupting or fragmenting whole virus, infectious (wild-type or attenuated) or non-infectious (for example inactivated), with a disrupting concentration of a splitting agent. The disruption results in a full or partial solubilisation of the virus proteins, altering the integrity of the virus. Preferably, the splitting agent is a non-ionic or an ionic surfactant. Accordingly, the split SARS viras foαnulations of the invention may also comprise at least one non-ionic surfactant or detergent. Examples of splitting agents useful in the invention include: bile acids and derivatives thereof, non-ionic surfactants, alkylglycosides or alkylthioglycosides and derivatives thereof, acyl sugars, sulphobetaines, betains, polyoxyethylenealkylethers, N,N-dialkyl-Glucamides, Hecameg, alkylphenoxypolyethoxyethanols, quaternary ammonium compounds, sarcosyl, CTAB (cetyl trimethyl ammonium bromide) or Cetavlon. Preferably, the ionic surfactant is a cationic detergent. Cationic detergents suitable for use in the invention include detergents comprising a compound of the following formula: R 1\ + R 3 R 2 / Ri x ~ wherein Ri, R 2 and R 3 are the same or different and each signifies alkyl or aryl, or Ri and R 2 , together with the nitrogen atom to which these are attached form a 5- or 6- membered heterocyclic ring, and R 3 signifies alkyl or aryl, or Ri, R 2 and R 3 together with the nitrogen atom to which these are attached, signify a 5- or 6- membered heterocyclic ring, unsaturated at the nitrogen atom, R 4 signfies alkyl or aryl, and X signifies an anion. Examples of such cationic detergents are cetyltrimethylammonium salts, such as ceytltrimethylammonium bromide (CTAB) and myristyltrimethylammonium salt. Additional cationic detergents suitable for use in the invention include lipofectine, lipofectamine, and DOT-MA. Non-ionic surfactants suitable for use in the invention include one or more selected from the group consisting of the octyl- or nonylphenoxy polyoxyethanols (for example the commercially available Triton series), polyoxyethylene sorbitan esters (Tween series) and polyoxyethylene ethers or esters of the general formula : O(CH 2 CH 2 O) n -A-R wherein n is 1-50, A is a bond or -C(O)-, R is Ci-so alkyl or phenyl Ci-so alkyl; and combinations of two or more of these. The invention comprises a method of preparing a split SARS viras comprising contacting the SARS viras with a sufficient amount of splitting agent to disrapt the viral envelope. The loss of integrity after splitting renders the virus non-infectious. Once the disrupted viral envelope proteins are generally no longer associated with whole intact virions, other viral proteins are preferably fully or partially solubilized and are therefore not associated, or only in part associated, with whole intact virions after splitting. The method of preparing a split SARS viras may further comprise removal of the splitting agents and some or most of the viral lipid material. The process may also include a number of different filtration and/or other separation steps such as ultracentrifugation, ultrafiltration, zonal centrifugation and chromatographic steps in a variety of combinations. The process may also optionally include an inactivation step (as described above) which may be carried out before or after the splitting. The splitting process may be carried out as a batch, continuous, or semi- continuous process. Split SARS viras vaccines of the invention may include structual proteins, membrane fragments and membrane envelope proteins. Preferably, the split SARS viras preparations of the invention comprise at least half of the viral structural proteins. One example of a method of preparing a split SARS virus formulation includes the following steps: (i) propagation of the SARS viras in cell culture, such as MRC-5 cells (ATCC CCL-171), WI-38 cells (ATCC CCL-75), fetal rhesus kidney cells or vero cells (See the discussion in Section A, above, regarding culture of SARS virus); (ii) harvesting of SARS virus-containing material from the cell culture; (iii) clarification of the harvested material to remove non-SARS viras material; (iv) concentration of the harvested SARS virus; (v) separation of the whole SARS virus from non- viras material; (vi) splitting of the whole SARS virus using a suitable splitting agent in a density gradient centrifugation step; and (vii) filtration to remove undesired materials. The above steps are preferably performed sequentially. The clarification step is preferably performed by centrifugation at a moderate speed. Alternatively, a filtration step may be used for example with a 0.2μm membrane. The concentration step may preferably employ an adsorption method, for instance, using CaHPO 4 . Alternatively, filtration may be used, for example ultrafiltration. A further separation step may also be used in the method of the invention. This further separation step is preferably a zonal centrifugation separation, and may optionally use a sucrose gradient. The sucrose gradient may further comprise a preservative to prevent microbial growth. The splitting step may also be performed in a sucrose gradient, wherein the sucrose gradient contains the splitting agent. The method may further comprise a sterile filtration step, optionally at the end of the process. Preferably, there is an inactivation step prior to the final filtration step. Methods of preparing split SARS virus formulations may further include treatment of the viral formulation with a DNA digesting enzyme. These enzymes may be used to reduce the level of host cell DNA in the viral purification process. DNA digesting enzymes for use in cell culture are known in the art and include, for example, Benzonase ® . Treatment of the SARS virus formulation with a DNA digesting enzyme may occur at any time in the purification and splitting process. Preferably, however, the SARS virus formulation is treated with a DNA digesting enzyme prior to use of a detergent. Still more preferably, the SARS virus formulation is treated with a DNA digesting enzyme, such as Benzonas, prior to treatment with a cationic detergent, such as CTAB. Methods of purification of split virus are known in the art. See JP Gregersen "Herstellung von Virussimpfstoffen aus Zellkulturen" Chapter 4.2 in Pharmazeutische Biotecnologie (eds. O. Kayser and RH Mueller) Wissenschaftliche Verlagsgesellschaft, Stuttgart, 2000. The invention includes a split vaccine composition comprising a prophylactically effective amount of SARS viral antigen, preferably spike or an immunogenic fragment thereof. The SARS viral antigen is preferably present in a concentration amount of 0.1 to 50 μg antigen/dose, more preferably 0.3 to 30 μg antigen/dose. Still more preferably, the antigen is about 15 μg/dose. In one embodiment, a lower concentration of SARS viral antigen is used in split vaccine compositions of the invention. Such lower concentration vaccines may optionally comprise an adjuvant to boost the host immune response to the antigen. In such a "low dose" vaccine, the SARS viral antigen is preferably present in a concentration of less than 15 μg antigen dose, (i.e., less than 10, 7.5, 5 or 3 μg antigen/dose. D. Subunit SARS Vaccines The invention includes a composition comprising an isolated or purified SARS viral antigen or a derivative thereof. The composition may further comprise one or more adjuvants. SARS viral antigens can be isolated or purified from a SARS virus grown in cell culture. Alternatively, SARS viral antigens can be recombinantly produced by methods known in the art. The SARS viral antigens used in the invention can be produced in a variety of different expression systems which are known in the art; for example those used with mammalian cells, baculoviruses, bacteria, and yeast. Such expression systems will typically use polynucleotides encoding the viral antigens of the invention. Such sequences can be obtained using standard techniques of molecular biology, including translating the amino acid sequences listed herein. Accordingly, the invention includes polynucleotides encoding for the viral antigens of the invention. In addition, the viral antigens of the invention can be produced (at least in part, preferably in whole) via synthetic chemistry methods. Insect cell expression systems, such as baculovirus systems, are known to those of skill in the art and described in, e.g., Summers and Smith, Texas Agricultural Experiment Station Bulletin No. 1555 (1987). Materials and methods for baculoviras/insert cell expression systems are commercially available in kit form from, inter alia, Invitrogen, San Diego CA. Similarly, bacterial and mammalian cell expression systems are also known in the art and described in, e.g., Yeast Genetic Engineering (Bao et al., eds., 1989) Butterworths, London. A number of appropriate host cells for use with the above systems are also known. For example, mammalian cell lines are known in the art and include immortalized cell lines available from the American Type Culture Collection (ATCC), such as, but not limited to, Chinese hamster ovary (CHO) cells, HeLa cells, baby hamster kidney (BHK) cells, monkey kidney cells (e.g., Hep G2), Madin-Darby bovine kidney ("MDBK") cells, as well as others. Mammalian sources of cells include, but are not limited to, human or non-human primate (e.g., MRC-5 (ATCC CCL-171), WI-38 (ATCC CCL-75), fetal rhesus lung cells (ATCC CL-160), human embryonic kidney cells (293 cells, typically transformed by sheared adenovirus type 5 DNA), VERO cells from monkey kidneys), horse, cow (e.g., MDBK cells), sheep, dog (e.g., MDCK cells from dog kidneys, ATCC CCL34 MDCK (NBL2) or MDCK 33016, deposit number DSM ACC 2219 as described in WO 97/37001), cat, and rodent (e.g., hamster cells such as BHK21-F, HKCC cells, or Chinese hamster ovary cells (CHO cells)), and may be obtained from a wide variety of developmental stages, including for example, adult, neonatal, fetal, and embryo. Similarly, bacterial hosts such as E. coli, Bacillus subtilis, and Streptococcus spp., will find use with the present expression constructs. Yeast hosts useful in the present invention include, inter alia, Saccharomyces cerevisiae, Candida albicans, Candida maltosa, Hansenual polymorpha, Kluyveromyces fragilis, Kluyveromyces lactis, Pichia guillerimondii, Pichia pastoris, Schizosaccharomyces pombe and Yarrowia lipolytica. Insect cells for use with baculovirus expression vectors include, inter alia, Aedes aegypti, Autographa californica, Bombyx mori, Drosophila melanogaster, Spodopterafrugiperda, and Trichoplusia ni. Nucleic acid molecules comprising nucleotide sequences of the viral antigens or antibodies of the invention can be stably integrated into a host cell genome or maintained on a stable episomal element in a suitable host cell using various gene delivery techniques well known in the art. See., e.g., US Patent No. 5,399,346. Depending on the expression system and host selected, the molecules are produced by growing host cells transformed by an expression vector under conditions whereby the protein is expressed. The expressed protein is then isolated from the host cells and purified. If the expression system secretes the protein into growth media, the product can be purified directly from the media. If it is not secreted, it can be isolated from cell lysates. The selection of the appropriate growth conditions and recovery methods are within the skill of the art. The invention includes a composition comprising an isolated or purified SARS viral antigen or a derivative thereof. The invention also includes a composition comprising at least two isolated or purified SARS viral antigens or derivatives thereof, which have been co-purified or purified separately and then combined. In one embodiment, the SARS viral antigen is a spike (S) protein. In yet another embodiment, the SARS viral antigen is a nucleocapsid (N) protein, a membrane (M) glycoprotein, or an envelope (E) protein. Preferably, the SARS viral antigen is present in the composition in a purity greater than 75% (e.g., 78%, 80%, 82%, 85%, 88%, 90%-, 92%, 95%, 98%). The invention includes a vaccine composition comprising a prophylactically effective amount of SARS viral antigen, preferably spike or an immunogenic fragment thereof. The SARS viral antigen is preferably present in a concentration amount of 0.1 to 50 μg antigen/dose, more preferably 0.3 to 30 μg antigen/dose. Still more preferably, the antigen is about 15 μg/dose. In one embodiment, a lower concentration of SARS viral antigen is used in vaccine compositions of the invention. Such lower concentration vaccines may optionally comprise an adjuvant to boost the host immune response to the antigen. In such a "low dose" vaccine, the SARS viral antigen is preferably present in a concentration of less than 15 μg antigen/dose, (i.e., less than 10, 7.5, 5 or 3 μg antigen/dose. The following example illustrates a method of preparing a SARS virus spike (S) protein subunit vaccine. SARS viras S antigen may be isolated and purified from a variety of sources and using a variety of methods, including, but not limited to, S antigen expressed in cultured eukaryotic cells (e.g., mammalian cells, such as VERO, CHO) or bacteria (e.g., E. coli). Expression of may be achieved by a variety of means, such as, for example, from SARS viras infected cell culture or cell culture supematants, from cultured cells stably transformed with a DNA expression cassette encoding the SARS virus S protein (e.g., RNA polymerase U promoter operably linked to a SARS virus S gene), or from cultured cells infected with a replication-competent or replication- incompetent virus-based expression vector (e.g., adenovirus vector, poxvirus vector, alphavirus vector, retrovirus vector) encoding the SARS virus S protein, as a means to eliminate the need to work with infectious SARS virus. 1. Subunit SARS Vaccines Produced from SARS Viras Cultures The SARS viras may be grown in cultured mammalian celle, such as VERO cells, then separated from the cultured cells. A SARS viral antigen, such as the S protein, can then be solubilized and separated from the SARS viras, and further isolated and purified. In one example, the SARS virus may be produced as described in the Inactivated SARS vaccine examples, then the desired SARS antigen, such as spike protein, may be further purified from the end product using techniques known in the art. In another example, a SARS subunit vaccine may be produced as follows. SARS virus may be produced using a desired mammalian cell line on microcarrier beads in large, controlled fermentors. For example, vaccine quality African Green Monkey kidney cells (VERO cells) at a concentration of 10 5 cells/mL are added to 60 to 75 L of CMRL 1969 media, pH 7.2, in a 150 L bioreactor containing 360 g of Cytodex-1 microcarrier beads and stioed for 2 hours. Additional CMRL 1969 is added to give a total volume of 150 L. Fetal bovine seram (FBS) is added to a final concentration of 3.5%. Glucose is added to a final concentration of 3.0 g/L and glutamine is added to a final concentration of 0.6 g/L. Dissolved oxygen, pH, agitation and temperature are controlled, and cell growth, glucose, lactate and glutamine levels are monitored. When cells are in logarithmic phases usually on days 3 to 4 reached a density of about 1.0-2.5xl0 6 cells/mL, the culture medium is drained from the fermentor and 120 L of CMRL 1969, pH 7.2 (no FBS) is added and the culture stioed for 10 minutes. The draining and filling of the fermentor is usually repeated once but could be repeated up to three times. After washing the cells, the fermentor is drained and 50 L of CMRL 1969 containing 0.1% (v/v) FBS is added. The SARS virus inoculum is added at a multiplicity of infection (m.o.i.) of 0.001 to 0.01. Trypsin may be added to promote efficient infection. Additional CMRL 1969 with 0.1% FBS is added to give a final volume of 150 L. Incubation is continued at 34 C. One viral harvest is obtained from a single fermentor lot, typically at 2-7 days post-infection. Multiple harvests from a single fermentation may also be obtained. The isolation and purification of S protein may be effected by a variety of means, as described below. For example, collecting S protein-containing flow-through from ion exchange chromatography of solubilized SARS virus envelope proteins; loading the flow through onto a hydroxyapatite matrix, and selectively eluting the S protein from the hydroxyapatite matrix. The selectively eluted S protein may be further concentrated by tangential flow ultrafiltration. Alternatively, the isolation and purification may be effected by collecting S protein- containing flow-through from ion exchange chromatography of the solubilized SARS viras envelope proteins; loading the flow through onto a hydroxyapatite matrix and collecting an S protein-containing flow through, selectively removing detergent used in the solubilization step from the hydroxyapatite matrix flow through to provide isolated and purified S protein. The isolated and purified S protein may be subsequently concentrated by tangential flow ultrafiltration Nucleic acid contaminants may be removed from the isolated and purified S protein by treatment with a nucleic acid degrading agent as described above in the Inactivation section. Preferably, the nucleic acid degrading agent is a nuclease, such as for example, Benzonase. The isolated and purified S protein may be applied to a gel filtration medium and the S protein subsequently collected therefrom to separate the S protein from contaminants of other molecular weights. Alternatively, the isolation and purification may be effected by loading S protein on a first ion-exchange medium while permitting contaminants to pass through the medium, eluting the S protein from the first ion-exchange medium, to separate the S protein from contaminants of other molecular weights. The eluted S protein is applied to a second ion-exchange medium while allowing contaminants to pass through the second ion-exchange medium. The S protein is subsequently eluted therefrom, to provide the isolated and purified S protein. The eluted S protein may be concentrated by tangential flow ultrafiltration. Alternatively, substantially pure SARS viras S protein suitable for use as an immunogen in a subunit vaccine formulation may be prepared from infected cell lysates, such as for example using a non-denaturing detergent buffer containing 1% Triton X-100 and deoxycholate to lyse infected cells. The cell lysates are clarified by centrifugation and S protein is purified from the cell lysates by immunoaffinity purification. A monoclonal antibody against the S protein is generated and coupled to beads and a column is constructed with those beads. SARS-infected cell lysates are applied to the column, and the column is washed with PBS containing 0.1% Triton X-100. Protein bound to the column is eluted with 0.1M glycine, pH 2.5, 0.1%) Triton X- 100. Elution samples are buffered, such as for example, with Tris, and analyzed for the presence of protein. Fractions containing the protein are pooled and dialyzed against PBS As discussed above, the present invention includes isolated and purified S protein of SARS virus. In one example, the virus is grown on a vaccine quality cell line, such as VERO cells, and the grown virus is harvested. The virus harvest is filtered and then concentrated typically using tangential flow ultrafiltration using a membrane of desired molecular weight cut-off and diafiltered. The viras harvest concentrate may be centrifuged and the supernatant discarded. The pellet from the centrifugation then is detergent extracted to solubilize the S protein, for example, ) by resuspending the pellet to the original harvest concentrate volume in an extraction buffer containing a detergent such as a non-ionic detergent including TRITON X-100. Following centrifugation to remove non-soluble proteins, the S protein exfract is purified by chromatographic procedures. The extract may first be applied to an ion exchange chromatography column such as a TMAE-fractogel or S-fractogel column equilibrated to permit the S protein to flow through while impurities are retained on the column. Next, the flow through may be loaded onto a hydroxyapatite column, equilibrated to permit binding of the S protein to the matrix and to permit contaminants to pass from the column. The bound S protein is then eluted from the column by a suitable elutant. The resulting purified solution of S protein may be further processed to increase its purity. The eluate first may be concentrated by tangential flow ultrafiltration using a membrane of desired molecular weight cut-off. The filtrate may be contacted with a polyethylene glycol of desired molecular weight, for example, about 6000 to 8000, to precipitate the protein. Following centrifugation and discard of the supernatant, the pellet may be resuspended in PBS and dialyzed to remove the polyethylene glycol. Finally, the dialyzed solution of S protein may be sterile filtered. The sterile filtered solution may be adsorbed onto alum. The polyethylene glycol precipitation and resuspension purification step may be effected at an earlier stage of the purification operation, if desired. Alternatively, SARS virus is recovered following growth and harvesting of the virus, and a concentrate obtained such as, for example using PEG precipitation or tangential flow filtration. The viras is contacted with detergent to solubilize the S proteins. Following centrifugation, the supernatant is recovered to further purification of the S protein and the non-soluble proteins discarded. The supernatant is applied to an ion exchange chromatography column, such as a TMAE- fractogel or S-fractogel column, suitably equilibrated to permit retention of the S protein on the column. The S protein is eluted from the ion-exchange column under suitable conditions. The eluate then may be passed through a gel filtration column, such as a Sephacryl S-300 column, to separate the S protein from contaminants of other molecular weights. A hydroxyapatite column may be employed in place of the Sephacryl column. The S protein may be eluted from the column to provide a purified solution of S protein. The eluate may be concentrated by tangential flow ultrafiltration using a membrane of desired molecular weight cut-off. The concentrated S protein solution then may be sterile filtered. Alternatively, viral harvests may be concentrated by ultrafiltration and the concentrated viral harvests may be subjected to an initial purification step, for example, by gel filtration chromatography, polyethylene glycol precipitation or Cellufine sulfate chromatography. The purified virus may then be detergent extracted to solubilize the S protein. Following solubilization of the S protein, the supernatant may be loaded onto an ion-exchange column such as Cellufine sulfate chromatography column equilibrated to permit the protein to bind to the column while permitting contaminants to flow through. Similarly, a TMAE-fractogel or S- fractogel column may be used in place of the Cellufine sulfate column. The two columns also may be combined in sequential purification steps. The S protein is eluted from the columns to provide a purified solution of the protein. This solution may be concentrated by tangential flow ultrafiltration using a membrane of desired molecular weight cut-off and diafiltered. Specifically, in one method of S protein purification, the virus harvest concentrate is centrifuged at 28,000 x g for 30 minutes at 4 C. The supernatant is discarded and the pellet resuspended in extraction buffer consisting of 10 mM Tris-HCl, pH 7.0, 150 mM NaCl, 2% (w/v) Triton X-100 to the original harvest concentrate volume. Pefabloc is added to a final concentration of 5 mM. The suspension is stioed at room temperature for 30 minutes. The supernatant, containing the soluble S protein, is clarified by centrifugation at 28,000 x g for 30 minutes at 4 C. A TMAE-Fractogel column is equilibrated with 10 mM Tris-HCl, pH 7.0, 150 mM NaCl containing 0.02% Triton X-100. The Triton X-100 supernatant, containing the soluble S protein, is loaded directly onto the TRAE-Fractogel column. The total volume added plus 2 bed volumes of 10 mM Tris-HCl, pH 7.0, 150 mM NaCl containing 0.02% Triton X-100 are collected. The TMAE—Fractogel flow-through containing S protein is diluted 3-fold with 10 mM Tris-HCl, pH 7.0, containing 0.02% Triton X-100. An hydroxyapatite column is equilibrated with 10 mM Tris-HCl, pH 7.0, 50 mM NaCl, 0.02%) Triton X-100. After loading the TMAE flow-through, the column is washed with 2 column volumes of 10 mM Tris-HCl, pH 7.0, 50 mM NaCl , 0.02% Triton X-100 followed by 4 column volumes of 5 mM sodium phosphate, pH 7.0, 1M NaCl, 0.02% Triton X-100. The proteins are eluted with 4 column volumes of 20 mM sodium phosphate, pH 7.0, 1M NaCl , 0.02% Triton X-100. Fractions are collected based on A280 and the protein content and antigen concentrations are measured. The purified S protein is ultrafiltered by tangential flow ultrafiltration using a 300 kDa NMWL membrane. 2. Recombinant Production of Subunit SARS Vaccines As discussed above, SARS virus proteins may be produced by recombinant expression. Host cells suitable for recombinant expression include bacterial, mammalian, insect, yeast, etc. Recombinant expression may be used to produce a full length SARS protein, a fragment thereof, or a fusion therewith. Fusion peptides may be used to facilitate the expression and purification of the recombinant SARS protein. For example, recombinant production of the SARS polypeptides can be facilitated by the addition a tag protein to the SARS antigen to be expressed as a fusion protein comprising the tag protein and the SARS antigen. Such tag proteins can facilitate purification, detection and stability of the expressed protein. Tag proteins suitable for use in the invention include a polyarginine tag (Arg-tag), polyhistidine tag (His-tag), FLAG-tag, Strep-tag, c-myc-tag, S-tag, calmodulin-binding peptide, cellulose-binding domain, SBP-tag„ chitin- binding domain, glutathione S-transferase-tag (GST), maltose-binding protein, transcription termination anti-te niniantion factor (NusA), E. coli thioredoxin (TrxA) and protein disulfide isomerase I (DsbA). Prefeoed tag proteins include His-tag and GST. A full discussion on the use of tag proteins can be found at Terpe et al., "Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems", Appl Microbiol Biotechnol (2003) 60:523-533. 5 After purification, the tag proteins may optionally be removed from the expressed fusion protein, i.e., by specifically tailored enzymatic treatments known in the art. Commonly used proteases include enterokinase, tobacco etch virus (TEV), thrombin, and factor X a . Accordingly, the invention further includes a SARS virus subunit vaccine comprising a fusion protein. Preferably, the fusion protein comprises a first amino acid sequence encoded by 10 a SARS virus polynucleotide sequence. SARS viras polynucleotide sequences which may encode said first amino acid sequence include one or more of the SARS virus polynucleotide sequences identified in this application and fragments thereof. The fusion protein may comprise an amino acid sequence of a SARS virus protein or a fragment thereof. Said SARS virus protein may be selected from one or more of the group L5 consisting of the following SARS viras proteins: P28, P65, Nspl, Nsp2 (3CL protease), Nsp3, Nsp3, Nsp4, Nsp 5, Nsp6, Nsp 7, Nsp 8, Nsp 9 (RNA polymerase), Nsp 10 (helicase), Nsp 11, Nsp 12, Nsp 13, Spike, Orf 3, Orf 4, Envelope, Matrix, Orf 7, Orf 8, Orf 9, Orf 10, Orf 11, Nucleocapsid and Orf 13. In one embodiment, the fusion protein comprises a first amino acid sequence comprising a O SARS virus antigen or a fragment thereof. Said SARS virus amino acid sequence may comprise one or more of the T-epitope sequences identified above. Preferably, the fusion protein comprises an amino acid sequence of a SARS viras spike protein, or a fragment thereof. Specific fragments of the spike protein which may be used in the fusion protein include the SI domain and the S2 domain. Further fragments of the spike protein 5 which may be used in the fusion protein include regions of each of the S 1 and S2 domains, including the receptor binding region of the SI domain, the oligomerization domain regions of the S2 domain, the leucine zipper regions of the S2 domain, the membrane anchor region of the S2 domain, the hydrophobic domain region of the S2 domain, the cystein-rich domain region of the S2 domain, and the cytoplasmic tail region of the S2 domain. (See FIGURE 19). Amino 0 acid sequences of the Spike protein cooesponding to these regions can be identified by those skilled in the art, including, for example, using the functional predictions set forth earlier in the application (predicted transmembrane helices, predicted N-terminus signaling regions, predicted coiled-coil regions, etc.) as well as by homology comparison to the sequences of other known Coronaviruses (See FIGURES 4F and 5). 5 The fusion protein may further comprise a second amino acid sequence. Said second amino acid sequence may comprise a polypeptide sequence which facilitates protein expression or purification, preferably one of the tag sequences discussed above. Alternatively, said second amino acid sequence may comprise a second amino acid sequence from a SARS viras. Alternatively, said second amino acid sequence may comprises an amino acid sequence from another virus or bacteria, including one or more of the viruses or bacteria identified in Section I, below. Said second amino acid sequence may comprise an amino acid sequence from another respiratory virus. Said second amino acid sequence may comprise an amino acid sequence from a virus selected from the group consisting of coronavirus, influenza virus, rhinovirus, parainfluenza virus (PIN), respiratory syncytial viras (RSN), adenovirus, and metapneumovirus. In one embodiment, said second amino acid sequence may comprise an amino acid sequence from an adjuvant, including one or more of the adjuvants identified in section I, below. In one embodiment, the invention includes a fusion protein comprising an amino acid sequence of a SARS virus spike protein or a fragment thereof. The fusion protein may further comprise a second amino acid sequence comprising an amino acid sequence selected from the group consisting of a second SARS virus protein, a non-SARS viras protein, a bacterial protein, and an adjuvant. (a) Bacterial Expression of Subunit SARS Vaccines hi one embodiment, bacterial host cells are used for recombinant expression of SARS viras proteins. Bacterial host cells suitable for use in the invention include, for example, E. coli, Bacillus subtilis, and Streptococcus spp. The SARS viral protein may be modified to facilitate bacterial recombinant expression. In particular, the SARS spike protein may be modified to facilitate transport of the spike protein to the surface of the bacterial host cell. Applicants have discovered that there is strong structural homology between the SARS viras spike protein and the ΝadA protein of Neisseria meningitidis. Both proteins have an Ν- teoninal globular "head" domain (amino acids 24-87), an intermediate alpha-helix region with high propensity to form coiled-coil structures (amino acids 88-350), and a C-terminal membrane anchor domain formed by four amphipatix transmembrane beta strands (amino acids 351-405 of ΝadA). In addition, a leucine zipper motive is present within the coiled-coil segment. See, FIGURE 19 depicting the SARS spike protein structure Comanducci et al, "ΝadA, a Novel Vaccine Candidate of Neisseria meningitidis", J. Exp. Med. 195 (11): 1445-1454 (2002). In addition, a leucine zipper motif of NadA is present within the coiled-coil segment. The NadA protein also forms high molecular weight surface-exposed oligomers (cooesponding to three or four monomers) anchored to meningococcal outer membrane. When the NadA protein is expressed in E. coli, the full-length protein is assembled in oligomers anchored to the outer membrane of E. coli, similar to the way the protein is presented in meningococcus. The NadA protein devoid of the predicted membrane anchor domain is then secreted into the culture supernatant. This secreted protein is soluble and still organized in trimers. The invention therefore includes a fusion protein comprising an amino acid sequence of a 5 SARS viras spike protein or a fragment thereof and a second amino acid sequence of a bacterial adhesion protein or a fragment thereof. Preferably, said adhesion protein is selected from the group consisting of NadA, YadA (of enteropathogenic Yersinia), andUspA2 (of Moraxella catarrhalis). Additional NadA-like proteins include serum resistance protein DsrA of Haemophilus ducreyi, the immunoglobulin binding proteins EibA, C, D, and F of E. coli, outer .0 membrane protein 100 of Actinobacillus actinomycetemcomitans, the saa gene carried on the large virulence plasmid present in shiga toxigenic strains of E. coli (STEC), and each of the bacterial adhesion proteins described in U.K. Patent Application No. 0315022.4, filed on June 26, 2003, each of which are specifically incorporated herein by reference. Preferably, said adhesion protein comprises NadA or a fragment thereof. L5 Such fusion proteins may be used to facilitate recombinant expression of immunogenic portions of SARS surface antigens, such as spike. These fusion constructs may also allow the SARS SI and/or S2 domains to adapt to a native confirmation. These fusion proteins are also able to oligomerize and form dimers or trimers, allowing the SI and/or S2 domains to associate and adapt conformations as in the native SARS spike protein. Further, these expression 20 constructs facilitate surface exposure of the SARS spike protein. The fusion proteins of the invention preferably comprise a leader peptide from a NadA like protein, preferably NadA, a polypeptide from the immunogenic "head" region of the spike protein, and a stalk region from either the NadA like protein or the Spike protein. During expression and processing of the fusion protein, one or more amino acids may be cleaved off or 25 removed, such as, i.e., the leader peptide or a membrane anchor domain. The stalk regions facilitate oligomerization of the expression protein. Optionally, the fusion proteins of the invention further include an anchor region of a NadA like protein. This anchor region allows the expression fusion protein to anchor and assemble on the bacterial cell surface. 0 The fusion proteins of the invention include the following constructs: (i) the NadA leader peptide (optionally also including the first 6 amino acids of the mature NadA protein to facilitate processing of the leader peptide and appropriate maturation of the protein) followed by the Spike SI domain. Preferably, this construct comprises amino acids 1- 29 of NadA (cooesponding to the NadA leader peptide and the first 6 amino acids of the mature 5 NadA protein, as shown in FIGURE 22 and as set forth below) followed by amino acids 14-662 of a SARS virus Spike protein (corresponding to the SI domain, see FIGURE 19 and SEQ ID NO: 6042 and as set forth below). Specifically, construct (i) comprises SEQ ID NO: 7302. (ii) the NadA leader peptide (optionally also including the first 6 amino acids of the mature NadA protein to facilitate processing of the leader peptide and appropriate maturation of the protein) followed by the Spike S 1 domain, followed by the stalk and anchor membrane domains of NadA. Preferably, this construct comprises amino acids 1-29 of NadA (cooesponding to the NadA leader peptide and the first 6 amino acids of the mature NadA protein, as shown in FIGURE 22 and as set forth below) followed by amino acids 14-662 of a SARS viras Spike protein (cooesponding to the SI domain, see FIGURE 19 and SEQ ID NO: 6042 and as set forth below) followed by amino acids 88-405 of NadA (cooesponding to the stalk and the anchor membrane domains). Specifically, construct (ii) comprises SEQ JD NO: 7303. (iii) the NadA leader peptide (optionally also including the first 6 amino acids of the mature NadA protein) followed by a SARS viras Spike SI domain, followed by the NadA stalk domain. Preferably, this construct comprises amino acids 1-29 of NadA followed by amino acids 14-662 of a SARS viras Spike protein (cooesponding to the SI domain), followed by amino acids 88-350 of NadA (cooesponding to the stalk domain). Specifically, construct (iii) comprises SEQ JD NO: 7304. (iv) the NadA leader peptide (optionally also including the first 6 amino acids of the mature NadA protein), followed by a SARS viras Spike SI and S2 domain (excluding the putative transmembrane region), followed by the anchor domain of NadA. Preferably, this construct comprises amino acids 1-29 of NadA, followed by amino acids 14-1195 of a SARS viras Spike protein (corresponding to SI and S2, excluding the putative transmembrane region), followed by amino acids 351-405 of NadA (cooesponding to the NadA anchor domain). Specifically, construct (iv) comprises SEQ JD NO: 7305. Alternatively, the NadA anchor domain may comprise amino acids 332 - 405 of NadA. (v) the NadA leader peptide (optionally also including the first 6 amino acids of the mature NadA protein), followed by a SARS virus Spike SI and S2 domain (exclusing the putative transmembrane region). Preferably, this construct comprises amino acids 1-29 of NadA, followed by amino acids 14-1195 of a SARS virus Spike protein. Specifically, construct (v) comprises SEQ ID NO: 7306. In each of constructs (i) to (v), the first 23 amino acids are the NadA leader peptide, and the GS dipeptide at residues 679-680 arises from the insertion of a restriction enzyme site. In constructs (i), (ii) and (iii), the NadA "head" is replaced by the Spike SI domain, and the fusion proteins are anchored to the outer membrane of E.coli or secreted in the culture supernatant, respectively. In constructs (iv) and (v), the "head" and "stalk" domains of NadA are replaced by SI and S2 Spike domains; also in this case, the two fusion proteins are anchored to the outer membrane of E.coli or secreted in the culture supernatant, respectively. Accordingly, the invention further includes a fusion protein comprising an amino acid sequence of a SARS viras spike protein or a fragment thereof and a second amino acid sequence of a bacterial adhesion protein or a fragment thereof. Preferably, amino acids corresponding to the "head" of the adhesion protein are replaced by amino acids cooesponding to a SARS viras Spike SI domain. Alternatively, the amino acids cooesponding to the "head" and "stalk" domains of the bacterial adhesion protein are replaced by amino acids corresponding to the SARS virus spike protein SI and S2 domains. As discussed above and shown in Figure 19, the SI domain of the Spike protein is identified as the globular receptor binding "head" region. The SI domain of the Spike protein preferably comprises about amino acids 14-662 of SEQ JD NO: 6042. The SI domain may comprise a shorter amino acid sequence, wherein amino acids are removed from either the N- terminal or C-terminal regions. Preferably, 3, 5, 7, 9, 13, 15, 20 or 25 amino acids are removed from either the N-terminal or C-terminal regions. The SI domain further includes amino acid sequences having sequence identity to the SI region of SEQ JD NO: 6042. An example of the SI domain is SEQ JD NO: 7307: As discussed above and shown in Figure 19, the S2 domain of the Spike protein is identified as the "stalk" region. The "stalk" region comprises oligomerization domain regions, a leucine zipper domain regions, membrane anchor regions, hydrophobic domain regions, cystein- rich domain region and a cytoplasmic tail region. The S2 domain of the Spike protein preferably excludes the transmembrane region and comprises about amino acids 663-1195 of SEQ ID NO: 6042. The S2 domain may comprise a shorter amino acid sequence, wherein amino acids are removed from either the N-terminal or C-terminal regions. Preferably, 3, 5, 7, 9, 13, 15, 20 or 25 amino acids are removed from either the N-terminal or C-terminal regions. The S2 domain further includes amino acid sequences having sequence identity to the S2 region of SEQ ID NO: 6042. An example of the SI domain (with the transmembrane region excluded) is SEQ JD NO: 7308. An example of the NadA protein described above is SEQ JD NO: 7309. As discussed above, the leader sequence of NadA used in the fusion protein preferably comprises about the first 29 amino acids of NadA (including a leader sequence with about 6 amino acids of the NadA head protein). Examples of such a leader sequences are set forth as SEQ JD NOS: 7310 and 7311 below. The fusion protein may use a leader sequence comprising a shorter amino acid sequence, wherein amino acids are removed from either the N-terminal or C-terminal regions. Preferably, 1, 2, 3, 4, or 5 amino acids are removed from either the N-terminal or C-terminal end of the sequence. The leader sequence used in the fusion protein may also include an amino acid sequences having sequence identity to SEQ ID NO: 7310 or SEQ ID NO: 7311. Preferably, the leader sequence comprises SEQ ID NO: 7311. Optionally, the fusion peptide comprises about the first 6 amino acids of the mature NadA protein to facilitate processing of the leader peptide and appropriate maturation of the protein. An examples of the first 6 amino acids of a mature NadA proteins is SEQ JD NO: 7312.. As discussed above, the stalk and anchor sequences of NadA used in the fusion protein preferably comprise about amino acids 88-405 of NadA. An example of an amino acid sequence comprising NadA stalk and anchor regions is set forth below as SEQ JD NO: 7313 below. An example of an amino acid sequence comprising a NadA stalk region (without the anchor region) is set forth as SEQ JD NO: 7314 below. An example of an amino acid sequence comprising a NadA anchor region is set forth as SEQ JD NO: 7315 below. The fusion protein may use a stalk (and/or anchor) sequence comprising a shorter amino acid sequence, wherein amino acids are removed from either the N-terminal or C-terminal regions. Preferably, 1, 2, 3, 4, 5, 6, 7, 8 or 9 amino acids are removed from either the N-terminal or C-terminal end of the sequence. The leader sequence used in the fusion protein may also include an amino acid sequences having sequence identity to the SEQ JD NO: 7313. The fusion proteins of the invention, including those described above, may be prepared, for example, as follows. Single fragments (such as the regions described above) may be amplified by PCR using the oligonucleotide primers set forth in the Table below. (S 1 1 refers to the Spike protein fused to the leader peptide of NadA; S2 refers to the stalk region of the Spike protein, with and without the stop codon). The oligonucleotides were designed on the basis of the DNA sequence of NadA from N. meningitidis B 2996 strain and of Spike from SARS viras isolate FRA1. Each oligonucleotide includes a restriction site as a tail in order to direct the cloning into the expression vector pET21b. SEQ ID NO: Restriction site S1 L For 7316 Ndel S1 L Rev 7317 BamHI S2 For 7318 Bamffl S2 Rev 7319 Hindm S2-stop Rev 7320 Xhol NadA 88 For 7321 Bamffl NadA 350 Rev 7322 Xhol NadA 332 For 7323 Hindm NadA 405 Rev 7324 Xhol The single fragments are sequentially cloned into pET21b vector, in order to express the proteins under the control of inducible T7 promoter. The SI domain of the Spike protein fused to the leader peptide of NadA (S1 L ) was obtained by PCR using the primers SI L -FOΓ and S1 L - Rev. The forward oligonucleotide primer contains the Ndel restriction sequence and the sequence coding for the leader peptide of NadA plus the first 6 aminoacids of the mature protein. The PCR fragment was cloned as a Ndel/BamEJJ fragment in the pET21b vector opened with the same restriction enzymes. This clone (PET-SI L ) was then used to sequentially clone the other different domains, as BamHJ/XhoI, BamHJ/HindlJJ or HindlTJ/XhoI fragments. Bamffl and HindJH restriction sites introduce the aminoacids GS and KL, respectively. The PCR amplification protocol was as follows: 200ng of genomic DNA from Neisseria meningitidis 2996 or 10 ng of plasmid DNA preparation (plasmid pCMVnew, containing the entire gene coding of the Spike protein), were used as template in the presence of 40μM of each oligonucletide primer, 400-800 μM dNTPs solution, lx PCR buffer (including 1.5mM MgCl 2 ), 2.5 units Taql DNA polymerase (using Perkin-Elmer AmpliTaQ or Invitrogen Platinum Pfx DNA polymerase). After a preliminary 3 minute incubation of the whole mix at 95 °C, each sample underwent a two-step amplification: the first 5 cycles were performed using the hybridisation temperature that excluded the restriction enzyme tail of the primer (Tml). This was followed by 30 cycles according to the hybridisation temperature calculated for the whole length oligos (Tm2). Elongation times, performed at 68°C or 72°C, varied according to the length of the fragment to be amplified.The cycles were completed with a 10 minute extension step at 68°C or 72°C. The amplified DNA was either loaded directly on agarose gel and the DNA fragment cooesponding to the band of correct size was purified from the gel using the Qiagen™ Gel Extraction Kit, following the manufacturer's protocol. The purified DNA corresponding to the amplified fragment and the plasmid vectors were digested with the appropriate restriction enzymes, purified using the QIAquick™ PCR purification kit (following the manufacturer's instructions) and ligation reactions were . performed. The ligation products were transformed into competent E. coli DH5α and screening for recombinant clones was performed by growing randomly-selected colonies and extracting the plasmid DNA using the Qiagen QIAprep Spin Miniprep Kit, following the manufacturer's instructions. Recombinant plasmids were introduced into E. coli BL21(DE3) used as expression host. Single recombinant colonies were inoculated into LB + ampicillin and incubated at 37°C for 14- 16 h. Bacteria were directly recovered by centrifugation (uninduced conditions) or diluted in fresh medium and grown at 37°C until OD 600 between 0.4-0.8. Protein expression was induced by addition of 1 mM Isopropyl- 1-thio-β-D-galactoρyranoside (LPTG) for three hours (induced conditions). Whole cell lysates were obtained resuspending bacteria in SDS-sample buffer IX and boiling for 5-10 min. Equal amounts of proteins were separated using NuPAGE (Invitrogen) or BIORAD Gel System, according to the manufacturer's instructions. Proteins were revealed by Coomassie-blue staining or transferred onto nitrocellulose membranes for western blot analysis. Western blot was performed using a rabbit polyclonal anti-serum against purified NadA Λ35 i -405 (diluted 1:3000) and a secondary peroxidase-conjugate antibody (DAKO). Results of the expression in E.coli of S1L, SlL-NadA and Sl -NadAΔanch or are shown in FIGURES 38 and 39. Schematics of the fusion constructs are shown in FIGURE 37. Bacterial expression of the SARS viral antigens may also be used to prepare compositions comprising outer membrane vesicles wherein said outer membrane vesicles comprise one or more SARS viral antigens. Outer Membrane Vesicles ("OMV"), also referred to as blebs, refer to vesicles formed or derived from fragments of the outer membrane of a Gram negative bacterium. OMVs typically comprise outer membrane proteins (OMPs), lipids, phospholipids, periplasmic material and lipopolysaccharide (LPS). Gram negative bacteria often shed OMVs during virulent infections in a process known as blebbing. OMVs can also be obtained from Gram negative bacteria via a number of chemical denaturation processes, such as detergent extraction. Synthetic OMVs or liposomes, comprising a lipid bilayer and typically enclosing an aqueous core, can also be prepared with the SARS viral antigens of the invention. The OMVs of the invention are preferably lipid vesicles comprising a lipid bilayer suoounding an aquous core. Typically the lipid vesicles are of unilamellar structure (i.e., a single lipid bilayer surrounds the aquous core), although multilammelar lipid vesicles may also be used in the compositions of the invention. OMVs typically have sizes in the nanomolar to micromolar range, e.g., from 1 nM to 100 μM, more typically from lOnM to 10 μM and preferably from 30 nM to 1 μM. The OMVs of the invention are preferably prepared from gram negative bacteria. Gram negative bacteria are those bacteria that fail to resist decolorization in the commonly known Gram staining method. Gram negative bacteria are characterized by a complex multilater cell wall and often possess an outer layer polysaccharide capsule. Gram negative bacteria suitable for producing OMVs include, for example, species from Neisseria, Moraxella, Kingella, Acinetobacter, Brucella, Bordetella, Chlamydia, Porphyromonas, Actinobacillus, Borelia, Serratia, Campylobacter, Helicobacter, Haemophilus, Escherichia, Legionella, Salmonella, Pseudomonas and Yersinia. The OMVs of the invention preferably comprise one or more SARS viral antigens or a fragment thereof. The SARS viral antigens may be recombinantly expressed in a Gram negative bacterial host cell and then harvested with the OMV. Antigenic components, such as recombinantly expressed SARS viral antigens, may be located in any or all of the three main compartments of the lipid vesicles, including attached to either the interior or exterior surface of the lipid vesicle, for example via a membrane anchor domain, or attachment to a lipid moiety; inserted into the lipid bilayer, for example where the antigenic component is itself a hydrophobic or lipid based entity; or located within the aqueous center or core of the lipid vesicle. Synthetically prepared OMVs, or liposomes, may be used in the invention. Such liposomes may comprise a number of different lipids and fatty acids. Suitable lipids for inclusion in liposomes of the invention include but are not limited to phophatidylinositol-(4,5)- diphosphate, phosphatidylserine, phosphatidylcholine, phosphatidylethanolamine, phosphatidyglycerol, cholesterol, beta-oleolyl-gamma-palmitoyl, lipopolysaccharides and galactocerbrosides. Suitable means for extraction of OMVs from bacterial sources include deoxycholate extraction, Tris/HCl/EDTA extraction, and lithium acetate extraction. Preferably, the extraction process comprises a physical and/or chemical means to disrupt the bacterial cell outer membrane in order to release sufficient OMVs for purification and isolation. See, e.g., WO 03/051379. The OMVs of the invention may be enriched and/or supplemented with antigenic components, such as SARS viral antigens, by methods known in the art, including, for example, direct combination in vitro where an energetic combination step can optionally be applied to facilitate integration of the antigenic component into a compartment of the liposome. Methods of energetic combination suitable for use in the invention include homogenization, ultrasonication, extrusion, and combinations thereof. Preferably, the antigenic component, such as the SARS viral antigen, is recombinantly produced by the host cell from which the OMV is derived. In one embodiment, such OMVs are prepared by introducing nucleic acid sequence encoding for the SARS viral antigen into the recombinant host cell. Preferably the nucleic acid sequence encoding for the SARS viral antigen is controlled by a strong promoter sequence. Preferably, the nucleic acid sequence encoding the SARS viral antigen further comprises an outer-membrane targeting signal. For example, the nucleic acid sequence encoding the SARS viral antigen may be fused to a sequence encoding for a naturally occurring outer membrane protein of the bacterial host. Preferably, the nucleic acid sequence encoding the SARS viral antigen is fused to the signal peptide sequence of the naturally occurring outer membrane protein of the bacterial host. Methods of preparing an optimizing OMVs for use in vaccines are disclosed in, for example Filip et al, J. Bact. (1973) 115: 717-722; Davies et al, J. Immunol. Method (1990) 143:215-225; and WO 01/09350. In one embodiment, a bacterial host cell, such as E. coli, are transformed to express the SARS spike protein. As discussed above, the spike protein may be modified to facilitate bacterial expression and transport of the spike protein to the surface of the host cell. Each of the Spike/NadA fusion constructs discussed above may be used in the OMV preparations of the invention. Preferably, constructs comprising the spike SI globular head domain fused to the stalk region of NadA are used to generate OMVs. The construct may optionally include the NadA leader peptide as well as the NadA anchor peptide. Schematic diagrams of these prefeoed OMV constructs are depicted in FIGURE 49. Example 6 describes one method of preparing the OMVs of the invention. (b) Mammalian Expression of Subunit SARS Vaccine As discussed above, mammalian host cells may be used for recombinant expression of SARS virus proteins. Mammalian host cells suitable for use in the invention include, for example, Chinese hamster ovary (CHO) cells, HeLa cells, baby hamster kidney (BHK) cells, monkey kidney cells (e.g., Hep G2), Madin-Darby bovine kidney ("MDBK") cells, as well as others. Mammalian sources of cells include, but are not limited to, human or non-human primate (e.g., MRC-5 (ATCC CCL-171), WI-38 (ATCC CCL-75), human embryonic kidney cells (293 cells, typically transformed by sheared adenovirus type 5 DNA), VERO cells from monkey kidneys (including, for example COS7 cells), horse, cow (e.g., MDBK cells), sheep, dog (e.g., MDCK cells from dog kidneys, ATCC CCL34 MDCK (NBL2) or MDCK 33016, deposit number DSM ACC 2219 as described in WO 97/37001), cat, and rodent (e.g., hamster cells such as BHK21-F, HKCC cells, or Chinese hamster ovary cells (CHO cells)), and may be obtained from a wide variety of developmental stages, including for example, adult, neonatal, fetal, and embryo. . The polynucleotides encoding the SARS viral proteins may be modified to facilitate or enhance expression. For example, commercial leader sequences known in the art, such as tPA or IgK or interleukin-2, may be used in the recombinant constructs. Preferably, however, the natural SARS leader sequence is used. Use of the natural leader sequence can be used to ensure that the protein will be trafficked in human cells in the same way as during a normal viral infection, which may be advantageous e.g. for DNA vaccines, where antigen is expressed in situ. As discussed above, tag sequences can be used in the expression constructs to facilitate purification, detection and stability of the expressed protein. Tag proteins suitable for use in the invention include a polyarginine tag (Arg-tag), polyhistidine tag (His-tag), FLAG-tag, Strep-tag, i c-myc-tag, S-tag, calmodulin-binding peptide, cellulose-binding domain, SBP-tag„ chitin- binding domain, glutathione S-fransferase-tag (GST), maltose-binding protein, transcription termination anti-terminiantion factor (NusA), E. coli thioredoxin (TrxA) and protein disulfide isomerase I (DsbA). Preferred tag proteins include His-tag and GST. A full discussion on the use of tag proteins can be found at Terpe et al, "Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems", Appl Microbiol Biotechnol (2003) 60:523-533. After purification, the tag proteins may optionally be removed from the expressed fusion protein, i.e., by specifically tailored enzymatic treatments known in the art. Commonly used proteases include enterokinase, tobacco etch viras (TEV), thrombin, and factor X a . One or more amino acid sequences or amino acid domains of the spike protein may be removed to facilitate mammalian recombinant expression. For instance, the entire S2 domain or the spike transmembrane region may be removed. Representative examples of some expression constructs of both full length and truncated spike glycoprotein suitable for mammalian expression are shown in FIGURE 40. Polynucleotide sequences representing each construct are shown in SEQ JD NOS 6578-6583. A description of each annotation is shown below: Clone Name Description Expression Constract nSh natural leader sequence SEQ JD NO: 6578 full length Spike histidine tag nS natural leader sequence SEQ JD NO: 6579 full length Spike nShΔTC natural leader sequence SEQ JD NO: 6580 Spike without transmembrane sequence histidine tag nSΔTC natural leader sequence SEQ JD NO: 6581 Spike without transmembrane sequence nS lh natural leader sequence SEQ JD NO: 6582 SI domain histidine tag nSl natural leader sequence SEQ JD NO: 6583 SI domain Cloned cDNA fragments that encompass full-length Spike coding sequences, as well as a Spike construct deleted of the ttansmembrane and cytoplasmic domains (TM-Cy-deleted Spike) for secretion were inserted into an expression vector pCMNIII to create nSh and nShΔTC, respectively. Both spike proteins were tagged with six histidine residues at the end of C- terminus to aid initial characterization of the expressed spike proteins. Similar sequences encoding full-length Spike or transmembrane and cytoplasmic domain deleted Spike, but without the histidine "tag" are readily substituted by one of skill in the art. The likely locations of the expressed spike constructs was assessed by separating expressed proteins into an aqueous fraction (AF) and a detergent fraction (DF) using the procedure shown in Figure 48, with results of western blot analysis shown in Figure 43. The above described vector constracts were evaluated for expression after transfection into COS7 cells. The constract expressing the full length spike protein remained in the cell membrane while the constract expressing the truncated spike protein was located either in the cytosol (Figure 43) or secreted into the cell medium (Figure 44). As shown in Figure 43, full-length spike protein is found in DF (membrane) in an aggregated form, while the truncated protein is found in AF (cytosol) as a monomer. As shown in Figure 44, deleted proteins (ShΔTC) are secreted, and a small fraction of full-length spike protein is detected in the medium by rabbit seram. Recombinantly expressed spike proteins may be oligomerized. When the spike proteins are to be used in a vaccine or to generate antibodies specific to the spike protein, they are preferably oligomerized. In order to obtain oligomerized spike protein, it is preferred to maintain the transmembrane domain in the recombinant expression construct. For example, FIGURE 41 illustrates a western blot of COS7 cell lysates comparing expressed nSh and nShΔTC using both anti-his tag and rabbit anti-S ARS antibodies. As shown full-length (nSh) aggregates, but the truncated (nShΔTC) spike protein does not. Antibody raised against the His- tagged protein recognizes full-length and truncated spike proteins in native and reduced forms. Rabbit antiserum recognizes spike protein only in non-reducing conditions. Spike aggregates or oligomers were present in larger amounts in the cell lysates from the expressed nSh constructs. Preferably, the oligomerized spike proteins form a homotrimer, as indicated in FIGURE 47 A further experiment, illustrated in FIGURE 42, demonstrates that the oligomerization of the expressed nSh constructs is likely due to a non-covalent linkage (and is likely not due to, for example, a disulfide bond). The oligomer dissociates into monomers at elevated temperature (80-100°C), but is stable in reducing conditions if not heated. It is further prefeoed that recombinantly expressed spike proteins are glycoslyated. Tunicamycin and glycosidases were used to assess glycosylation. FIGURE 45 illustrates that glycoslation of expressed spike proteins is not affected by removal of the transmembrane domain region. Both full-length (Sh) and truncated (ShΔTC) SARS spike proteins are glycosylated. Preferably, expression of the constructs of the invention is not toxic to the mammalian host cell. FIGURE 46 demonstrates that expression of the illustrated spike constracts is not toxic to the COS7 host cell. Methods for transfecting, expressing, culturing, isolating and purifying recombinant proteins from mammalian cell cultures are known in the art. For example, the SARS spike constructs of the invention may be expressed in 293 cells. These cells may be cultured and transfected in static or monolayer cultures. For rapid large-scale production of SARS protein antigens in sufficient quantities for in vitro and in vivo evaluation, including immunogenicity studies, large-scale transient fransfection of 293 (human embryonic kidney) cells may be used to obtain milligram quantities of the recombinant antigen(s). Alternatively, larger scale transfection of these cells may be performed with 293 cells in suspension culture. Preferably, the expressed SARS proteins are harvested from the transfected cells between 48 and 72 hours after transfection or even from 72 to 96 or more hours after transfection. Where the host cells are transfected with truncated spike expression constracts, the expressed spike protein is secreted from the host cells and collected from the cell media. After concentration, the spike protein may be purified from the media using, for example, GNA lectin followed by DEAE and ceramic hydroxyapatite column chromatography. Where the host cells are transfected with full length spike expression constracts, but rather is retained within the cells, and may be purified from triton X-100 detergent extracted cells. The full-length Spike protein can then be captured on GNA lectin, followed by hydroxyapatite and SP chromatography. Chinese Hamster Ovary (CHO) or other eukaryotic (e.g., mammalian) cells that stably express the SARS viral antigens of the invention may also be derived (e.g. Figure 73). Preferably, the cells are CHO cells, and these constracts will comprise one or more marker or selection genes in order to select for the desired CHO cells. In one embodiment, the constructs comprise a CMV enhancer/promoter, ampicillin resistance gene, and a fused DHFR and attenuated neomycin gene for selection purposes. Stable cell lines can then be produced using the neomycin selection system in CHOK-1 cells. Selected clones can then be sequenced to verify the integrity of the insert, and transient transfections can then be performed using Trans- LTl polyamine transfection reagent (PanVera Corp., Madison, WI) to assess the expression level and also the integrity of the expressed protein by ELISA and western blot analysis. Methods for derivation of CHO cells stably expressing the SARS viral antigens of the invention comprise the steps of transfection and primary screening with selective medium. Optionally, these steps are followed by subcloning to assure purity of cell lines. Cell culture supematants can be assayed using an antigen capture ELISA to quantify expression levels at all stages of selection and amplification. For full-length Spike expression constructs, methanol fixed cells can be screened for internal expression by immunofluorescent staining using a rabbit anti-SARS antibody. Successive measurements at the T75-flask stage of expansion can be employed to assure stability of expression levels. The molecular mass and integrity of the expressed proteins can be checked by PAGE both under native and reducing and denaturing conditions, followed by immunoprobing. In one embodiment, the pCMV3 vectors expressing SARS-CoV Spike proteins in either full-length or truncated forms is introduced into CHOK-1 cells using the Trans-LT-1 reagent. ) On day one, lxlO 6 cells are plated on 100 mm dishes in non-selective F12 media + 10% Fetal Bovine Serum + 4 mM Glutamine. On day two, the cells are transfected with a DNA:LT-1 mixture and the media then replaced with complete F12 media. Twenty-four to forty-eight hours later depending on the cell density, each 100 mm dish is split to 4-6 100 mm dishes. The medium is changed to complete selective media containing Geneticin (neomycin) at 500 μg/ml. All bovine seram used in these procedures is from TSE-free sources that meet cuoent FDA standards. Twenty-four hours later the medium is changed to complete selective medium plus 500 ug/ml neomycin. Ten to fourteen days later, individual colonies are picked and transferred to 96 well plates and cultured in complete selective medium but without G418. When approximately 80% of the wells are confluent, twenty-four hour supematants are screened by spike capture ELISA positive clones are transfeoed to twenty-four well plates. For the initial expression of full length Spike protein, methanol fixed cells will be screened by immunoflourescent staining using a rabbit anti-S ARS antibody. After the low expressing cell lines have been eliminated and there are less than 20-30 cell lines, capture ELISA and westerns will be used to determine the expression level after cell lysis. A portion of each cell line will be pelleted, weighed and lysed in 1% triton lysis buffer containing MOPS, NaCl and MgCl 2 at the same ratio of cell weight to lysis buffer. After lysis the supernatant is collected and expression level is determined. Three to four clones producing the highest levels of spike protein in correct stracture and conformation will be grown in three-liter bioreactors for expansion and adaptation to low seram suspension culture conditions for scale-up. The antigen capture ELISA assay for the SARS spike protein can be performed as described in the art. A brief description of this assay follows. 96 well flat-bottom plates (Coming, Coming, NY) are coated with 250ng per well of purified immunoglobulin obtained from rabbit sera that were immunized with inactivated SARS virus. Between steps, the plates are washed in a buffer containing 16%NaCl and 1% Triton X100. lOOμL of supernatant or lysate samples (diluted in a buffer containing lOOmM NaPO , 0.1% Casein, ImM EDTA, 1% Triton X100, 0.5M NaCl and 0.01 % Thiomersal, pH 7.5) are added and incubated for 2 hours at 37°C. Bound antigen is reacted against pooled SARS+ve serum or high affinity monoclonal antibody either human or mouse against SARS spike protein (1 hour incubation, 37°C) and detected using appropriate species-specific peroxidase conjugated second antibody (30 minute incubation at 37°C; TAGO, Burlingame, CA). The plates are developed for 15 minutes at room temperature using TMB substrate (Pierce, Rockford, JL) and the reaction stopped using 4N phosphoric acid. The plates are read at a wavelength of 450nm and the concentration of protein per ml sample is derived from a standard curve (OD vs. protein concentration) based on serial dilutions of a known concentration of recombinant spike protein. The immunoprobing analysis can also be performed following the standard methods described elsewhere in the art. A brief description follows. 10-20 μl of the sample is analyzed on 4-20% SDS PAGE under non-reducing/ denaturing conditions with mild heating. The gels are ran for 1.5-2.0 hours at 100V constant voltage. The proteins are then transferred onto nitrocellulose membranes (Millipore, Bedford, MA) for 45 min using the semidry western transfer system (BioRad, Hercules, CA) following the manufacturer's instructions. The membrane is then reacted against polyclonal anti-spike rabbit seram, followed by anti-rabbit Ig conjugated to Alexa 688 (Molecular Probes, Oregon). The blots are scanned using an infrared imaging system (Ll-Cor, Inc., Lincoln, Nebraska). The highest expressing candidate cell lines can be screened for spike protein expression and stability in small-scale (3 liter) suspension cultures. The candidate clone can be further evaluated for level of expression as well as integrity of expressed protein after amplification, and subsequently tested for expression stability in the absence of selection. The selected clones can also be tested for maintenance of the DNA sequence integrity of the integrated SARS spike protein gene. To quickly monitor the expression levels in small flask (T25 or T75) and in the three liter evaluation cultures, a lectin-based process (Gluvanthus Nivalis lectin) may be used to isolate SARS spike protein to a degree of purity that allows semi-quantitation and characterization of the protein in CHO supernatant. For full-length spike protein, it will be obtained from triton X-100 detergent extracted cells. Full-length Spike protein will be then captured on GNA lectin, followed by hydroxyapatite and SP chromatograph. Eluted protein is then characterized by: 1) polyacrylamide gel electrophoresis (PAGE) and Coomassie staining, 2) Immunoprobing with anti-SARS rabbit sera, 3) structural characterization using size exclusion chromatography (SEC), as well as mass spec analysis using MALDI-TOF. Routes and methods of immunization of the vaccines of the invention are discussed in more detail in a section below. Examples 7 to 9 illustrate sample immunization protocols for the recombinant spike proteins. Vaccine testing Prior to human administration, it is normal to test vaccines in animal models. A mouse model of SARS coronaviras infection is known (Subbarao et al. (2004) J Virol 78:3572-77), and other animals that may be used as models of infection and/or disease include ferrets and monkeys. Thus the invention provides a non-human animal that is infected by the SARS coronavirus, wherein the animal is preferably a ferret or a primate (e.g. a monkey or a macaque). The animal may be gnotobiotic. The animal is preferably not a cat (Felis domesticus). The animal may or may not display SARS disease symptoms e.g. ferrets (Mustela faro) show prominent pulmonary pathology after infection. See: Martina et al. (2003) Nature 425:915. E. Polynucleotides encoding the SARS Antigens of the Invention The invention includes polynucleotides encoding for the SARS antigens of the invention. In addition, the invention includes polynucleotides which have been optimized for recombinant production (e.g. codon optimization) of the SARS antigens of the invention, including polynucleotides encoding for each of the SARS fusion constructs discussed above. F. Viral vector or Viral Particle delivery of the SARS Antigens of the Invention The antigens of the invention may be expressed in vivo or in vitro by polynucleotides encoding the antigens. Expression and delivery of the polynucleotides of the invention may be facilitated via viral vectors and/or viral particles. 5 Gene-based delivery systems derived from viruses, such as alphavirases, are useful for the ex vivo and in vivo administration of heterologous genes, including one or more SARS genes, having therapeutic or prophylactic applications. These systems can also be used for the production of recombinant proteins derived from the SARS virus in cultured cells. Gene-based delivery systems of the invention include viral vectors (e.g., adenovirus vector, poxvirus vector, 0 alphaviras vector) and non- viral nucleic acid vectors (e.g., DNA, RNA) encoding one or more SARS viras antigens. Polynucleotides encoding SARS viras antigen(s) are incorporated into the gene-based vaccines individually or in combination (e.g., as bicistronic constructs). 1. Alphavirus Alphavirases are members of Togaviridae family and share common stractural and 5 replicative properties. Sindbis viras (SIN) is the prototype viras for the molecular study of other alphavirases, and together with Venezuelan equine encephalitis virus (VEE) and Semliki Forest virus (SFV), are the most widely utilized alphavirases being developed into expression vectors for heterologous genes (Schlesinger and Dubensky (1999) Curr Opin. Biotechnol. 70:434-439; Schlesinger (2001) Expert Opin. Biol. Ther. 1:177-91). ,0 Alphavirases possess a relatively small single-stranded RNA genome of positive polarity, which is approximately 12 kb in length, capped and polyadenylated. The RNA interacts with viral capsid protein monomers to form nucleocapsids, which in turn, are suoounded by a host cell-derived lipid envelope from which two viral glycoproteins, El and E2, protrude forming "spike" trimers of heterodimeric subunits. Two open reading frames (ORFs) encode as 5 polyproteins the enzymatic nonstructural replicase proteins (5' ORF) and the virion structural proteins (3' ORF). The structural polyprotein is translated from a highly abundant subgenomic mRNA, which is transcribed from a strong internal alphavirus promoter (Strauss and Strauss (1994) Microbiol. Rev. 58:491-562). Replication of the genome occurs exclusively within the host cell cytoplasm as RNA. 3 The most common alphavirus expression vectors have exploited both the positive-stranded nature and modular organization of the RNA genome. These vectors, termed "replicons" due to their property of self-amplification, permit insertion of heterologous sequences in place of the structural polyprotein genes, while maintaining the 5'- and 3 '-end cis replication signals, the nonstructural replicase genes, and the subgenomic junction region promoter (Xiong et al. (1989) 5 Science 243:1188-1191; Liljestrom (1991) Bio Technology 9:1356-1361). Chimeric alphavirus vectors (and particles) from sequences derived from divergent viras families have also been described, (see, for example United States patent application serial number 09/236,140; see also, US Patents 5,789,245, 5,842,723, 5,789,245, 5,842,723, and 6,015,694; as well as WO 95/07994, WO 97/38087 and WO 99/18226). Co-owned International Publication WO 02/099035, published December 12, 2002 and incorporated by reference in its entirety herein, describes chimeric alphavirus molecules and modified alphavirus molecules having modified Biosafety Levels. The absence of stractural protein genes renders alphavirus replicon vectors defective, in that RNA amplification and high-level heterologous gene expression occurs within the target cell, but cell-to-cell spread of vector is not possible due to the inability to form progeny virions. Through the years, several synonymous terms have emerged that are used to describe alphavirus replicon particles. These terms include recombinant viral particle, recombinant alphaviras particle, alphavirus replicon particle and replicon particle. However, as used herein, these terms all refer to a virion-like unit containing an alphavirus-derived RNA vector replicon. Moreover, these terms may be referred to collectively as vectors, vector constructs or gene delivery vectors. Packaging of replicon RNA into particles can be accomplished by introducing the replicon RNA into permissive cells (e.g., RNA or DNA transfection, or particle infection) that also contain one or more structural protein expression cassettes or "defective helper" constructs encoding the alphavirus structural proteins. These stractural protein encoding constracts may themselves be introduced into the cells by transfection of either RNA or DNA, and most commonly retain the native alphavirus subgenomic promoter, as well as 5'- and 3 '-end cis signals for co-amplification with the replicon, but are devoid of any replicase genes and the RNA packaging signal (Liljestrom (1991) Bio/Technology 9:1356-1361; Pushko et al. (1997) Virology 239:389-401; Polo et al. (1999) PNAS 96:4598-4603). Permanent cell lines that are stable transformed with constracts expressing the alphavirus structural proteins (e.g., packaging cell lines) offer a means to avoid transient transfection production methods (Polo et al. (1999) PNAS 9(5:4598-4603). The present invention includes compositions and methods for the production of replication defective viral vector particles (e.g., alphavirus replicon particles) for use in the ex vivo and in vivo administration of heterologous genes encoding proteins having therapeutic or prophylactic application, including genes encoding for one or more SARS viral antigens. In one aspect, the invention includes a method of producing replication defective viral vector particles (e.g., alphavirus replicon particles) comprising the steps of introducing at least one nucleic acid molecule comprising a viral vector (e.g., alphaviras replicon RNA) into immortalized cells of the present invention, under conditions that allow for complementation of the viral vector (e.g., alphavirus replicon RNA) and production of viral vector particles (e.g., alphavirus replicon particles), and isolating the viral vector particles from the cells or cell culture supematants. In certain embodiments, the immortalized cells are grown in suspension, for example PERC.6 cells. In other embodiments, the methods are performed in large-scale volumes, for example, liter volumes or greater, such as for example in roller bottles, large flasks, Nunc Cell Factories, Coming Cell Cubes, fermentation vessels, etc). hi certain embodiments, the viral vector is an alphaviras replicon RNA that requires complementation by providing one or more alphaviras structural proteins in trans, within the immortalized cell. In such instances, the methods of complementation to produce alphaviras replicon particles may involve the introduction of one or more nucleic acids (e.g., RNA, DNA) encoding said alphavirus stractural protein(s) (e.g., capsid and/or envelope glycoproteins) into the immortalized cells, either transiently or stably, and either concurrent with or prior to the introduction of the alphavirus replicon RNA. In certain embodiments, the alphaviras replicon RNA is introduced into the cell by transfection an in vitro transcribed RNA. In other embodiments, the alphavirus replicon RNA is introduced into the cell by transfection of a DNA (e.g., ELVIS), which is capable of transcribing within the cell, the replicon RNA. In yet other embodiments, the alphaviras replicon RNA is introduced into the cell by infection with a seed stock of alphavirus replicon particles. In certain embodiments, the nucleic acids encoding said alphavirus structural protein(s) are defective helper RNA or are DNA that can transcribe within the cell defective helper RNAs. As discussed herein, "alphaviras RNA replicon vector", "RNA replicon vector", "replicon vector" or "replicon" refers to an RNA molecule that is capable of directing its own amplification or self -replication in vivo, within a target cell. To direct its own amplification, the RNA molecule should encode the polymerase(s) necessary to catalyze RNA amplification (e.g., alphavirus nonstructural proteins nsPl, nsP2, nsP3, nsP4) and also contain cis RNA sequences required for replication which are recognized and utilized by the encoded polymerase(s). An alphavirus RNA vector replicon should contain the following ordered elements: 5' viral or cellular sequences required for nonstructural protein-mediated amplification (may also be refeoed to as 5' CSE, or 5' cis replication sequence, or 5' viral sequences required in cis for replication, or 5' sequence which is capable of initiating transcription of an alphavirus), sequences which, when expressed, code for biologically active alphavirus nonstructural proteins (e.g., nsPl, nsP2, nsP3, nsP4), and 3' viral or cellular sequences required for nonstructural protein-mediated amplification (may also be refeoed as 3' CSE, or 3' viral sequences required in cis for replication, or an alphavirus RNA polymerase recognition sequence). The alphavirus RNA vector replicon also should contain a means to express one or more heterologous sequence(s), such as for example, an IRES or a viral (e.g., alphaviral) subgenomic promoter (e.g., junction region promoter) which may, in certain embodiments, be modified in order to increase or reduce viral transcription of the subgenomic fragment, or to decrease homology with defective helper or structural protein expression cassettes, and one or more heterologous sequence(s) to be expressed. Preferably the heterologous sequence(s) comprises a protein- encoding gene, which is the 3' proximal gene within the vector replicon. And preferably the replicon further comprises a polyadenylate tract. As discussed herein, "recombinant Alphavirus Particle", "alphavirus replicon particle" and "replicon particle" refers to a virion-like unit containing an alphaviras RNA vector replicon. Generally, the recombinant alphavirus particle comprises one or more alphavirus stractural proteins, a lipid envelope and an RNA vector replicon. Preferably, the recombinant alphaviras particle contains a nucleocapsid stracture that is contained within a host cell-derived lipid bilayer, such as a plasma membrane, in which one or more alphaviral envelope glycoproteins (e.g., E2, El) are embedded. The particle may also contain other components (e.g., targeting elements such as biotin, other viral structural proteins or portions thereof, hybrid envelopes, or other receptor binding ligands), which direct the tropism of the particle from which the alphavirus was derived. Generally the interaction between alphavirus RNA and structural protein(s) necessary to efficiently form a replicon particle or nucleocapsid may be an RNA- protein interaction between a capsid protein and a packaging signal or packaging sequence contained within the RNA. "Alphavirus packaging cell line" refers to a cell which contains one or more alphaviras stractural protein expression cassettes and which produces recombinant alphavirus particles (replicon particles) after introduction of an alphaviras RNA vector replicon, eukaryotic layered vector initiation system, or recombinant alphavirus particle. The parental cell may be of mammalian or non-mammalian origin. Within prefeoed embodiments, the packaging cell line is stably transformed with the structural protein expression cassette(s). "Defective helper RNA" refers to an RNA molecule that is capable of being amplified and expressing one or more alphaviras stractural proteins within a eukaryotic cell, when that cell also contains functional alphavirus nonstructural "replicase" proteins. The alphaviras nonstructural proteins may be expressed within the cell by an alphavirus RNA replicon vector or other means. To permit amplification and stractural protein expression, mediated by alphavirus nonstructural proteins, the defective helper RNA molecule should contain 5 '-end and 3 '-end RNA sequences required for amplification, which are recognized and utilized by the nonstructural proteins, as well as a means to express one or more alphavirus structural proteins. Thus, an alphavirus defective helper RNA should contain the following ordered elements: 5' viral or cellular sequences required for RNA amplification by alphavirus nonstructural proteins (also referred to elsewhere as 5' CSE, or 5' cis replication sequence, or 5' viral sequences required in cis for replication, or 5' sequence which is capable of initiating transcription of an alphaviras), a means to express one or more alphavirus stractural proteins, gene sequence(s) which, when expressed, codes for one or more alphavirus structural proteins (e.g., C, E2, El), 3' viral or cellular sequences required for amplification by alphavirus nonstructural proteins (also referred to as 3' CSE, or 3' viral sequences required in cis for replication, or an alphaviras RNA polymerase recognition sequence), and a preferably a polyadenylate tract. Generally, the defective helper RNA should not itself encode or express in their entirety all four alphavirus nonstructural proteins (nsPl, nsP2, nsP3, nsP4), but may encode or express a subset of these proteins or portions thereof, or contain sequence(s) derived from one or more nonstructural protein genes, but which by the nature of their inclusion in the defective helper do not express nonstructural protein(s) or portions thereof. As a means to express alphaviras stractural protein(s), the defective helper RNA may contain a viral (e.g., alphaviral) subgenomic promoter which may, in certain embodiments, be modified to modulate transcription of the subgenomic fragment, or to decrease homology with replicon RNA, or alternatively some other means to effect expression of the alphaviras structural protein (e.g., internal ribosome entry site, ribosomal readthrough element). Preferably an alphavirus structural protein gene is the 3' proximal gene within the defective helper. In addition, it is also preferable that the defective helper RNA does not contain sequences that facilitate RNA-protein interactions with alphavirus structural protein(s) and packaging into nucleocapsids, virion-like particles or alphaviras replicon particles. A defective helper RNA is one specific embodiment of an alphavirus structural protein expression cassette. Alphaviras for use in the invention may be grown in any one of the cell lines discussed above as suitable for the SARS virus. Alphaviras replicon particles may be produced according to the present invention by using the above cell lines (e.g., immortalized cell lines) and a variety of published and accepted alphaviras vector methodologies. Such methodologies include, for example, transient packaging approaches, such as the co-transfection of in vitro transcribed replicon and defective helper RNA(s) (Liljestrom, Bio/Technology 9:1356-1361, 1991; Bredenbeek et al, J. Virol 67:6439- 6446, 1993; Frolov et al, J. Virol. 77:2819-2829, 1997; Pushko et al, Virology 239:389-401, 1997; US Patents 5,789,245 and 5,842,723) or co-transfection of plasmid DNA-based replicon and defective helper construct(s) (Dubensky et al, J. Virol. 70:508-519, 1996), as well as introduction of alphavirus stractural protein expression cassettes (e.g., DNA-based defective helper) into immortalized cell lines of the present invention to create stable packaging cell lines (PCL) (Polo et al, PNAS 96:4598-4603, 1999; US Patents 5,789,245, 5,842,723, 6,015,694; WO 97/38087, WO 99/18226, WO 00/61772, and WO 00/39318). Stable packaging cell lines may then be utilized for alphaviras replicon particle production. The PCL may be transfected with in vitro transcribed alphavirus replicon RNA, transfected with a plasmid DNA-based replicon (e.g., ELVIS vector), or infected with a seed stock of alphavirus replicon particles, and then incubated under conditions and for a time sufficient to produce progeny alphavirus replicon particles in the culture supernatant. In addition, progeny replicon particles can subsequently be passaged in additional cultures of naive PCL by infection, resulting in further expansion and commercial scale preparations. Importantly, by using defective helper RNA or stable PCL based on the "split" structural gene configuration, these replicon particle stocks may be produced free from 5 detectable contaminating RCV. Following harvest, crude culture supematants containing the chimeric alphavirus replicon particles may be clarified by passing the harvest through a filter (e.g., 0.2 uM, 0.45 uM, 0.65 uM, 0.8 uM pore size). Optionally, the crude supematants may be subjected to low speed centrifugation prior to filtration to remove large cell debris. Within one embodiment, an L0 endonuclease (e.g., Benzonase, Sigma #E8263) is added to the preparation of alphaviras replicon particles before or after a chromatographic purification step to digest exogenous nucleic acid. Further, the preparation may be concentrated prior to purification using one of any widely known methods (e.g., tangential flow filtration). Crude or clarified alphavirus replicon particles may be concentrated and purified by chromatographic techniques (e.g., ion exchange chromatography, 5 size exclusion chromatography, hydrophobic interaction chromatography, affinity chromatography), such as those described in WO01/92552, incorporated by reference in its entirety herein. Two or more such purification methods may be performed sequentially. EXAMPLE OF ALPHAVIRUS REPLICON PARTICLES ENCODING SARS VIRUS SPIKE (S) ANTIGEN 0 The invention includes compositions and methods for the production of replication defective viral vector particles (e.g., alphaviras replicon particles) for use in the ex vivo and in vivo administration of heterologous genes encoding proteins having therapeutic or prophylactic application, including genes encoding for one or more SARS viral antigens. The following example illustrates a method of preparing alphaviras replicon particles 5 encoding SARS virus spike (s) antigen. The SARS viras spike gene can be incorporated into alphaviras replicon particles derived from a variety of alphavirus, such as Sindbis viras, Semliki Forest virus (US 5739026), Venezuelan equine encephalitis virus (US 6531135), and replicon particle chimeras derived from more than one alphavirus (US 6376236, WO 02/99035). In addition, the SARS viras spike gene 3 can be incorporated in its entirety (encoding full-length spike protein) or in a modified form that includes, for example, sequence deletions or truncations, such that the encoded a spike protein is of less than full-length (e.g., C-terminal truncation of one or more (e.g. at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30 etc.) amino acids, deleted of transmembrane region and cytoplasmic tail). For example, the spike gene may be cloned as a full-length gene into the VCR-chim2.1 > vector (WO 02/99035) by standard RT-PCR conditions or by standard subcloning from one of the other plasmids described herein, using commercially available restriction endonucleases. For the reverse transcription step in standard RT-PCR, the Superscript pre-amplification kit (Invitrogen™) and the primer SEQ JD NO: 7325 (sp-RT-R) are used: For the amplification step, the cDNA polymerase advantage kit (Clonetech) and two primers Sp-F-BbvCI (SEQ ID NO: 7326) and Sp-R-Notl (SEQ JD NO: 7327) are used: The forward primer is designed to contain the ccacc sequence (Kozak, 1991 JBC 19867- 70) in front of the ATG codon to optimize translation efficiency of the spike gene. Also, the forward primer contains the BbvCI restriction site and the reverse primer contains the Notl restriction site for subsequent cloning of the PCR amplified gene. The PCR product is purified using the QIAquick Nucleotide Removal kit (QIAgen), digested with BbvCI and Notl, gel purified with QIAquick Gel Extraction kit (QIAgen), and ligated to plasmid VCR-Chim2.1 pre-digested with the same enzymes. Clones containing the SARS spike sequence are verified by sequencing and the new construct is called VCR-Chim2.1- SARSspike. To generate VEErep/SINenv-SARSspike replicon particles the plasmids VCR-Chim2.1- SARSspike, VCR-DH-Scap (WO 02/99035), and VCR-DH-Sglydll60 (WO 02/99035) are linearized with the restriction enzyme Pmel and used for in vitro transcription as described previously (Polo et al. 1999, PNAS 96: 4598-603; WO02/99035). The transcripts are cotransfected into BHK cells as previously described (Polo et al, 1999, ibid; WO02/99035). The transfected cells are incubated at 34 °C, the supematants collected at 20 and 30 hrs post- electroporation, clarified by centrifugation, and purified by chromatography as previously described (WO 01/92552). Expression of the SARS spike protein from the replicon particle vector is verified by infecting BHK cells overnight with purified VEErep/SINenv-SARSspike or VEErep/SINenv- GFP (WO 02/99035) replicon particles. In addition, BHK cells also were transfected in parallel with in vitro transcribed VCR-Chim2.1-SARSspike replicon RNA. At 16 hrs post-infection and transfection cells are lysed and a sample of the lysate analyzed by western blot using an antibody that recognizes SARS virus spike protein. The proteins on the gel are stained or transferred to a membrane for Western blot analysis with sera from convalescent patients or alternatively murine or rabbit antisera generated against SARS virus. VEErep/SINenv-SARSspike replicon particles are administered to the vaccine recipient (e.g., rodent, non-human primate, human) as described elsewhere in the present invention. Figure 67 shows data from western blot analysis performed under non-reducing conditions, using a SARS virus specific rabbit polycl