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Response,” Science, Jun. 25, 2010, pp. 1703-1705, vol. 328.","npl_type":"a","external_id":["pmc3156580","20508090","10.1126/science.1189801"],"record_lens_id":"017-446-438-518-052","lens_id":["019-283-822-128-971","074-876-575-179-082","017-446-438-518-052"],"sequence":38,"category":[],"us_category":[],"cited_phase":"APP","rel_claims":[]}},{"npl":{"num":27,"text":"Wu, J. et al., “Cyclic GMP-AMP Is an Endogenous Second Messenger in Innate Immune Signaling by Cytosolic DNA,” Science, Feb. 15, 2013, pp. 826-830, vol. 339.","npl_type":"a","external_id":["pmc3855410","10.1126/science.1229963","23258412"],"record_lens_id":"057-770-397-028-617","lens_id":["058-929-461-341-228","077-020-133-942-600","057-770-397-028-617"],"sequence":39,"category":[],"us_category":[],"cited_phase":"APP","rel_claims":[]}},{"npl":{"num":28,"text":"Wu, X. et al., “Molecular evolutionary and structural analysis of the cytosolic DNA sensor cGAS and STING,” Nucleic Acids Research, Jun. 12, 2014, pp. 8243-8257, vol. 42, No. 13.","npl_type":"a","external_id":["10.1093/nar/gku569","pmc4117786","24981511"],"record_lens_id":"051-693-185-968-805","lens_id":["068-280-428-540-080","156-046-133-862-263","051-693-185-968-805"],"sequence":40,"category":[],"us_category":[],"cited_phase":"APP","rel_claims":[]}},{"npl":{"num":29,"text":"Zeltins, A., “Construction and Characterization of Virus-Like Particles: A Review,” Mol Biotechnol, 2013, pp. 92-107, vol. 53.","npl_type":"a","external_id":["23001867","10.1007/s12033-012-9598-4","pmc7090963"],"record_lens_id":"058-690-248-817-352","lens_id":["154-661-339-503-858","153-285-543-583-266","058-690-248-817-352"],"sequence":41,"category":[],"us_category":[],"cited_phase":"APP","rel_claims":[]}},{"npl":{"num":30,"text":"Zimmermann, P. et al., “Characterization of Syntenin, a Syndecan-binding PDZ Protein, as a Component of Cell Adhesion Sites and Microfilaments,” Molecular Biology of the Cell, Feb. 2001, pp. 339-350, vol. 13.","npl_type":"a","external_id":["11179419","10.1091/mbc.12.2.339","pmc30947","011179419"],"record_lens_id":"090-804-834-044-439","lens_id":["143-178-494-540-609","090-804-834-044-439","179-240-619-711-899"],"sequence":42,"category":[],"us_category":[],"cited_phase":"APP","rel_claims":[]}},{"npl":{"num":31,"text":"Satoh, T. et al., “Gene Transduction in Human Monocyte-Derived Dendritic Cells Using Lentiviral Vectors,” Methods Mol Biol, 2013, pp. 401-409, vol. 960.","npl_type":"a","external_id":["23329503","10.1007/978-1-62703-218-6_30"],"record_lens_id":"049-354-173-164-983","lens_id":["099-628-490-675-233","071-871-959-355-709","049-354-173-164-983"],"sequence":43,"category":[],"us_category":[],"cited_phase":"APP","rel_claims":[]}},{"npl":{"num":32,"text":"Uzé, G. et al., “Domains of Interaction between Alpha Interferon and its Receptor Components,” J Mol Biol, 1994, pp. 245-257, vol. 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6253.","npl_type":"a","external_id":["pmc4617605","10.1126/science.aab3632","26229117"],"record_lens_id":"052-264-887-777-22X","lens_id":["162-273-101-998-032","189-502-663-087-333","052-264-887-777-22X"],"sequence":46,"category":[],"us_category":[],"cited_phase":"APP","rel_claims":[]}},{"npl":{"num":35,"text":"Gentili, M. et al. “Transmission of innate immune signaling by packaging of cGAMP in viral particles” Science, Sep. 11, 2015, pp. 1232-1236, vol. 349, No. 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musculus","tax_id":10090},{"name":"Homo sapiens","tax_id":9606}],"document_location":["DDESC"],"count":2,"data_source":["USPTO_FULLTEXT_RB","EMBLPAT_EBI","GBPAT_NCBI"]},"has_sequence":true,"legal_status":{"ipr_type":"patent for invention","granted":true,"earliest_filing_date":"2015-09-16","grant_date":"2018-07-03","anticipated_term_date":"2035-11-27","has_disclaimer":false,"patent_status":"ACTIVE","publication_count":2,"has_spc":false,"has_grant_event":true,"has_entry_into_national_phase":false},"abstract":{"en":[{"text":"The present invention relates to methods for preparing virus-like particles comprising immunogenic cyclic dinucleotides.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"}]},"abstract_lang":["en"],"has_abstract":true,"claim":{"en":[{"text":"1. A virus-like particle comprising a lipoprotein envelope comprising a viral fusogenic glycoprotein, wherein said virus-like particle contains cyclic guanosine monophosphate-adenosine monophosphate (cGAMP) packaged into said virus-like particle.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"2. The virus-like particle according to claim 1 , wherein the virus-like particle further comprises a capsid from retroviridae.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"3. The virus-like particle according to claim 2 , wherein the retroviridae capsid is from a lentivirus or retrovirus.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"4. The virus-like particle according to claim 2 , wherein the retroviridae capsid is from HIV or Murine Leukemia Virus (MLV).","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"5. The virus-like particle according to claim 1 , wherein the viral fusogenic glycoprotein is a glycoprotein from retroviridae, herpesviridae, poxviridae, hepadnaviridae, flaviviridae, togavoridae, coronaviridae, hepatitis D virus, orthomyxoviridae, paramyxoviridae, filoviridae, rhabdoviridae, bunyaviridae, or orthopoxiviridae.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"6. The virus-like particle according to claim 1 , wherein the viral fusogenic glycoprotein is a glycoprotein from Human Immunodeficiency Virus (HIV), HIV-1, HIV-2, Influenza virus, Influenza virus type A, Influenza virus type B, Thogotovirus, or Vesicular Stomatitis Virus (VSV).","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"7. The virus-like particle according to claim 1 , wherein the cyclic dinucleotides are 2′-3′-cyclic GMP-AMP.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"8. The virus-like particle according to claim 1 , wherein the cyclic dinucleotides are 3′-3′-cyclic GMP-AMP.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"9. The virus-like particle according to claim 1 , further comprising an antigen or a protein or nucleic acid of interest.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"10. The virus-like particle according to claim 1 as a drug or a vaccine adjuvant.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"11. A pharmaceutical, vaccine or veterinary composition comprising a virus-like particle according to claim 1 and a pharmaceutically acceptable carrier.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"12. The pharmaceutical, vaccine or veterinary composition according to claim 11 , further comprising an antigen or a therapeutically active agent.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"13. A method for inducing or enhancing an immune response in a subject comprising administering a virus-like particle according to claim 1 or a composition according to claim 11 .","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"14. A method for treating an infectious disease or a cancer in a subject comprising administering a virus-like particle according to claim 1 or a composition according to claim 11 .","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"15. A virus-like particle comprising a lipoprotein envelope comprising a viral fusogenic glycoprotein, wherein said virus-like particle contains cGAMP packaged into said virus-like particle wherein the virus-like particle contains at least 0.015 ng/ml of cGAMP.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"16. A pharmaceutical, vaccine or veterinary composition comprising a virus-like particle according to claim 15 and a pharmaceutically acceptable carrier.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"17. A method for preparing a virus-like particle comprising cyclic dinucleotides packaged into said virus-like particle, wherein the method comprises: co-expression of a cyclic GMP-AMP synthase (cGAS) and a viral fusogenic glycoprotein in a eukaryotic cell in conditions allowing the synthesis of cGAMP and the viral fusogenic glycoprotein in said cell; and recovering the virus-like particles produced by said cell, wherein the virus-like particles comprise cGAMP packaged into said virus-like particle.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"18. The method according to claim 17 , wherein said cell further expresses a capsid from retroviridae.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"19. The method according to claim 17 , wherein the viral fusogenic glycoprotein is a glycoprotein from retroviridae, herpesviridae, poxviridae, hepadnaviridae, flaviviridae, togavoridae, coronaviridae, hepatitis D virus, orthomyxoviridae, paramyxoviridae, rhabdoviridae, bunyaviridae, filoviridae, and orthopoxiviridae.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"20. The method according to claim 17 , wherein the viral fusogenic glycoprotein is a glycoprotein from HIV, HIV-1 and HIV-2, Influenza virus, Influenza virus type A, Influenza virus type B, Thogotovirus, or VSV.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"21. The method according to claim 17 , wherein the retroviral capsid is from a retroviridae.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"}]},"claim_lang":["en"],"has_claim":true,"description":{"en":{"text":"CROSS-REFERENCE TO RELATED APPLICATION This application claims the benefit of U.S. Provisional Application Ser. No. 62/051,016, filed Sep. 16, 2014, the disclosure of which is hereby incorporated by reference in its entirety, including all figures, tables and amino acid or nucleic acid sequences. The Sequence Listing for this application is labeled “Seq-List.txt” which was created on Sep. 14, 2015 and is 9 KB. The entire content of the sequence listing is incorporated herein by reference in its entirety. FIELD OF THE INVENTION The present invention relates to the field of medicine, in particular of vaccine. BACKGROUND OF THE INVENTION Cyclic dinucleotides have recently been described as potent cytosolic adjuvants of the immune system. They induce an antiviral innate immune response such as against HIV (Human Immunodeficiency Virus) and HSV (Herpes simplex virus), and also against cancer (WO2005/087238; WO2007/054279; WO2013/185052). Cyclic dinucleotides were previously identified in bacteria and known to be immunostimulatory. This field has recently gained a lot of attention following the identification that a cyclic dinucleotide, cGAMP (2′-3′-cyclic GMP-AMP), also exists in vertebrates and can be endogenously synthetized by the enzyme cGAS upon recognition of cytosolic DNA. Cyclic GMP-AMP synthase (cGAS) is a cytosolic DNA sensor that signals by catalyzing the synthesis of a second messenger, cGAMP. cGAS binds double-stranded DNA in a sequence non-specific manner and this induces a conformational change in its enzymatic site allowing for cyclic GMP-AMP (cGAMP) synthesis ((Wu et al., 2012 , Science, 339, 826-830; Sun et al., 2012 , Science, 339, 786-791; WO2014/099824; Ablasser et al., 2013 , Nature, 498, 380-384). Metazoan cGAMP bears both a canonical 3′-5′ and an unusual 2′-5′ phosphodiester bond. cGAMP binds and activates stimulator of interferon genes (STING). STING plays a central role in cytosolic DNA sensing by relaying a signal from upstream DNA sensors to activate transcription factors such as IRF3, which in turn drive IFN gene transcription. Interferons (IFN) play pivotal roles in the immune response to virus infection. IFN expression is induced by signaling pathways activated by sensors of virus presence, including cytosolic DNA sensors. However, cyclic dinucleotides do not efficiently cross the plasma membranes of cells and have a limited potency when used without vectors. Current vectors mainly consist of lipid-based complexes such as lipofectamine, which have limited use in vivo due to their toxicity. Therefore, there is a strong need for a vectorization means of cyclic dinucleotides, especially the promising cGAMP. SUMMARY OF THE INVENTION The present invention provides a new vectorization of cyclic dinucleotides, especially cGAMP, using enveloped virus-like particles. Indeed, cyclic dinucleotides, especially cGAMP, can be packaged into enveloped virus-like particles (VLPs) or virions and induce an innate immune response, in particular an interferon response, upon infection of cells. More particularly, in order to be able to vectorize cyclic dinucleotides, especially cGAMP, the VLPs need to be enveloped so as to optimize the delivery of cyclic dinucleotides, especially cGAMP, by fusion of VLP with the target cells. The present invention relates to a virus-like particle comprising a lipoprotein envelope including a viral fusogenic glycoprotein, wherein said virus-like particle contains cyclic dinucleotides packaged into said virus-like particle. Preferably, the virus-like particle further comprises a capsid from retroviridae. Preferably, the viral fusogenic glycoprotein is a glycoprotein from retroviridae (including lentivirus and retrovirus), herpesviridae, poxviridae, hepadnaviridae, flaviviridae, togaviridae, coronaviridae, hepatitis D virus, orthomyxoviridae, paramyxoviridae, filoviridae, rhabdoviridae, bunyaviridae, or orthopoxiviridae (e.g., variola), preferably from orthomyxovirus, retroviruses, or rhabdovirus. In particular, the viral fusogenic glycoprotein can be a glycoprotein from HIV (Human Immunodeficiency Virus), including HIV-1 and HIV-2; influenza, including Influenza A (e.g., subtypes H5N1 and H1N1) and Influenza B; thogotovirus; or VSV (Vesicular Stomatitis Virus). Preferably, the retroviral capsid is from retroviridae, preferably lentivirus and retrovirus. More preferably, the retroviral capsid is from HIV or MLV (Murine Leukemia Virus). Preferably, the cyclic dinucleotides are selected from the group consisting of cyclic di-adenosine monophosphate (c-di-AMP), cyclic di-guanosine monophosphate (c-di-GMP), and cyclic guanosine monophosphate-adenosine monophosphate (cGAMP). More preferably, the cyclic dinucleotides are cGAMP (2′-3′-cyclic GMP-AMP) or cGAMP (3′-3′-cyclic GMP-AMP). Optionally, the virus-like particle of the invention may further comprise an antigen or any other protein or nucleic acid of interest. The present invention relates to the virus-like particle as disclosed herein as a drug, especially a vaccine, or a vaccine adjuvant. It also relates to a pharmaceutical, vaccine or veterinary composition comprising a virus-like particle as disclosed herein, a pharmaceutically acceptable carrier and optionally an antigen or a therapeutic active agent. The present invention further relates to a method for inducing or enhancing an immune response in a subject comprising administrating a virus-like particle as disclosed herein or a composition as disclosed herein. It also relates to a method for preventing or treating an infectious disease, in particular a viral infection, or a cancer in a subject comprising administrating a virus-like particle as disclosed herein or a composition as disclosed herein. It relates to a virus-like particle or a composition as disclosed herein for use for preventing or treating an infectious disease, in particular a viral infection, or a cancer in a subject. It relates to the use of a virus-like particle or a composition as disclosed herein for the manufacture of a medicament or vaccine for preventing or treating an infectious disease, in particular a viral infection, or a cancer in a subject. In another aspect, the present invention relates to an expression vector or a combination of expression vectors, comprising a sequence encoding a cyclic dinucleotide synthase and either a sequence encoding a viral fusogenic glycoprotein or a sequence encoding retroviridae capsid protein, or both. Preferably, the expression vector comprises a sequence encoding a cyclic dinucleotide synthase and both a sequence encoding a viral fusogenic glycoprotein and a sequence encoding retroviridae capsid protein. Preferably, the cyclic dinucleotide synthase is selected from the group consisting of the diadenylate cyclase, diguanylate cyclase and the cyclic GMP-AMP synthase. More preferably, it is cGAS (Cyclic GMP-AMP synthase). Optionally, the expression vector may further comprise a sequence encoding an antigen or any other protein or nucleic acid of interest, in particular a therapeutic active agent. Preferably, the expression vector is a plasmid, a baculovirus vector or a viral vector. More preferably, the viral vector is selected from the group consisting of an adenoviral vector, an adeno-associated virus-based vector, and a lentiviral vector. The present invention further relates to the expression vector or combination thereof as disclosed herein as a drug, especially a vaccine, or a vaccine adjuvant. It also relates to a pharmaceutical, vaccine or veterinary composition comprising an expression vector or combination thereof as disclosed herein and a pharmaceutically acceptable carrier. The present invention also relates to a method for inducing or enhancing an immune response in a subject, comprising administering an expression vector or combination thereof as disclosed herein or a composition pharmaceutical, vaccine or veterinary composition comprising such vectors. It relates to a method for preventing or treating an infectious disease or a cancer in a subject, comprising administering an expression vector or combination thereof as disclosed herein or a composition pharmaceutical, vaccine or veterinary composition comprising such vectors. It relates to an expression vector or combination thereof as disclosed herein or a composition pharmaceutical, vaccine or veterinary composition comprising such vectors for use for preventing or treating an infectious disease, in particular a viral infection, or a cancer in a subject. It relates to the use of an expression vector or combination thereof as disclosed herein or a composition pharmaceutical, vaccine or veterinary composition comprising such vectors for the manufacture of a medicament or vaccine for preventing or treating an infectious disease, in particular a viral infection, or a cancer in a subject. Another aspect of the present invention is a recombinant eukaryotic host cell comprising a sequence encoding a cyclic dinucleotide synthase and a sequence encoding a viral fusogenic glycoprotein or a sequence encoding retroviridae capsid protein or both. Preferably, the cyclic dinucleotide synthase is selected from the group consisting of the diadenylate cyclase, diguanylate cyclase and the cyclic GMP-AMP synthase. More preferably, it is cGAS (Cyclic GMP-AMP synthase). Preferably, the recombinant eukaryotic host cell comprises a sequence encoding a cyclic dinucleotide synthase and both a sequence encoding a viral fusogenic glycoprotein and a sequence encoding retroviridae capsid protein. Optionally, the recombinant eukaryotic host cell may further comprise a sequence encoding an antigen or any other protein or nucleic acid of interest. In a first aspect, one or several sequences selected from the sequence encoding the cyclic dinucleotide synthase, the viral fusogenic glycoprotein and the sequence encoding retroviridae capsid protein are episomal. Alternatively, one or several sequence selected from the sequence encoding the cyclic dinucleotide synthase, the viral fusogenic glycoprotein and the sequence encoding retroviridae capsid protein are integrated into the host cell chromosome. The present invention also relates to the recombinant eukaryotic host cell as disclosed herein as a drug or a vaccine adjuvant. It relates to a method for inducing or enhancing an immune response in a subject comprising administering a recombinant eukaryotic host cell as disclosed herein. It also relates to a method for preventing or treating an infectious disease or a cancer in a subject comprising administering a recombinant eukaryotic host cell as disclosed herein. The present invention further relates to a method for preparing a virus-like particle comprising cyclic dinucleotides packaged into said virus-like particle, wherein the method comprises: co-expression of a cyclic dinucleotide synthase and a viral fusogenic glycoprotein in a eukaryotic cell in conditions allowing the synthesis of cyclic dinucleotides and the viral fusogenic glycoprotein in said cell; andrecovering of the virus-like particles produced by said cell. Preferably, the cyclic dinucleotide synthase is selected from the group consisting of the diadenylate cyclase, diguanylate cyclase and the cyclic GMP-AMP synthase. More preferably, it is cGAS (Cyclic GMP-AMP synthase). Preferably, said cell further expresses a capsid from retroviridae. Preferably, the viral fusogenic glycoprotein is a glycoprotein from retroviridae (including lentivirus and retrovirus), herpesviridae, poxviridae, hepadnaviridae, flaviviridae, togaviridae, coronaviridae, hepatitis D virus, orthomyxoviridae, paramyxoviridae, rhabdoviridae, bunyaviridae, filoviridae, and orthopoxiviridae (e.g., variola), preferably from orthomyxovirus, retroviruses, and rhabdovirus. More particularly, the viral fusogenic glycoprotein can be a glycoprotein from HIV (Human Immunodeficiency Virus), including HIV-1 and HIV-2; influenza including Influenza A (e.g., subtypes H5N1 and H1N1) and Influenza B; thogotovirus; and VSV (Vesicular Stomatitis Virus). Preferably, the retroviral capsid is from retroviridae, preferably lentivirus and retrovirus, preferably from HIV or MLV (Murine Leukemia Virus). BRIEF DESCRIPTION OF THE DRAWINGS The patent or application file contains at least one drawing executed in color. Copies of this patent or patent application publication, with color drawing(s), will be provided by the Office upon request and payment of the necessary fee. FIGS. 1A-1F . HIV-1-GFP produced in cGAS-reconstituted 293T cells induces IFN in infected cells. (A) Schematic of the experimental setup. (B) HEK293 cells were transfected with the IFNβ promoter reporter (p125-F-Luc) and pRL-TK as a control. After 6-8 hours, cells were infected (MOI=1) with HIV-1-GFP from producer cells expressing cGAS as indicated or were left uninfected. F-Luc activity was analyzed after 24 hours and normalized to R-Luc. m-cGAS-AA is a catalytically inactive mutant. (C) HIV-1-GFP infected cells were washed after 24 hours and after an additional 48 hours, IFN in the supernatant was analyzed by bioassay (left) and cells were collected for FACS analysis. The percentage of GFP positive cells is shown (right). Wedges represent MOIs of 10, 5, 2, 1, 0.5 and 0.1. (D) RNA was extracted from cells infected as in (C) (MOI=1). The indicated mRNAs were quantified relative to 18S rRNA by RT Q-PCR. (E) BMDMs of the indicated genotypes were infected with HIV-1-GFP (MOI=5) or Sendai virus (SeV, wedges represent MOIs of 1, 0.5 and 0.1). Supernatant was tested after 24 hours for mIFNα by ELISA. n.d., not detectable. (F) BMDMs were infected as in (E) and the indicated mRNAs were quantified relative to GAPDH mRNA by RT Q-PCR. Black wedges represent MOIs of 5 and 1 and grey wedges MOIs of 1, 0.5 and 0.1. Bars show the average of two (B,D,E) or four (C,F) replicates and error bars represent the range (B,D,E) or standard deviation (C,F). FIGS. 2A-2F . HEK293 cells express STING and induce IFN in response to cGAMP. (A) Cell extracts from THP1 and HEK293 cells were tested by Western blot for STING expression. An irrelevant intervening lane was spliced out during preparation of the figure. (B) 2×10 5 HEK293 cells were transiently transfected with the IFNβ promoter reporter (p125-F-Luc) and with pRL-TK as a control. After 24 hours, cells were transfected with 2 μg 2′-3′-cGAMP or with lipofectamine only (control). Luciferase activity was analyzed after 24 additional hours and F-Luc activity is shown normalized to R-Luc. Bars show the average of two replicates and error bars represent the range. IFN bioassay. (C) HEK293 cells were transduced with pGreenFire-ISRE using lentiviral delivery. Clones were obtained by serial dilution and, based on the responses to IFN, clone 3C11 was selected. 25,000 3C11 cells were seeded in 96-well plates and recombinant human IFNα2 was added. After 24 hours, cells were lysed and firefly luciferase activity was measured. Background bioluminescence in untreated cells was set to 1. Bars show the average of two replicates and error bars represent the range. Wild-type and mutant cGAS are expressed equally in virus producer cells. (D) 293T virus producer cells were lysed 72 hours after transfection and cGAS protein levels were determined by Western blot using a monoclonal antibody recognizing the FLAG-tag. Adenovirus-GFP (Ad-GFP) produced in cGAS-reconstituted cells does not trigger IFN in freshly infected target cells. (E) Ad-GFP was produced in HEK293 cells. Some virus producer cells were co-transfected with cGAS expression constructs. Virus stocks were then used to infect fresh HEK293 cells. Wedges represent 0.01 and 0.001 μl inoculum. IFN production by Ad-GFP infected cells was tested by bioassay. Recombinant IFNα at the indicated doses was used to demonstrate the responsiveness of the bioassay. Bars show the average of two replicates and error bars represent the range. (F) Infection was monitored by FACS. FIGS. 3A-3F . IFN induction triggered by HIV-1-GFP from cGAS expressing cells is independent of viral nucleic acids. (A) Virus stocks were treated or not with DNase I and then used to infect cells as in FIG. 1 (MOI=1). As controls, medium and m-cGAS plasmid were incubated with DNase I and then added to cells or transfected, respectively. (B) HIV-1-GFP was collected from producer cells transfected as indicated (supernatant, SUP). HIV-1-GFP was pelleted from an aliquot by centrifugation and resuspended in fresh medium (pelleted, PEL). Cells were then infected (MOI=1). (C) Cells were infected (MOI=1) in the presence of nevirapine (Nev) or raltegravir (Ral). The percentage of infected cells was determined by FACS (right). (D) Cells were infected with 100, 50 or 5 μl (wedges) supernatant from cells producing HIV-1-GFP or virus-like particles (VLPs). (E) HIV-1-GFP was pseudotyped with VSV-G or THOV-G and supernatants (VSV-G: 1 and 0.1 μl; THOV-G: 100 and 10 μl) from producer cells were used to infect cells. (F) HIV-1-GFP was produced in cells reconstituted with m-cGAS that were also treated with 20 μM GW4869 or 60 μM Ac-DEVD-CHO or were left untreated (control). Fresh cells were infected with 10, 1 or 0.1 μl (wedges) supernatant. In all panels, cells were infected for 24 hours, washed and after an additional 48 hours, IFN in the supernatant was analyzed by bioassay. Bars show the average of two (B,C,D,E), three (F) or four (A) replicates and error bars represent the range (B,C,D,E) or standard deviation (A,F). FIGS. 4A-4D . Small molecule extracts from HIV-1-GFP from cGAS-reconstituted producer cells induce IFN. (A) Schematic of the experimental setup. (B) Extracts from viruses produced in the absence of cGAS (first set of bars) or in the presence of wild-type or mutant cGAS (second and third sets of bars) were added to digitonin permeabilized THP1 cells. IFN in THP1 supernatants was assessed by bioassay. Gray wedges represent a 1:2 dilution series starting with extract from 10 7 infectious units. As controls, synthetic cGAMP was either directly added to THP1 cells (last set of bars) or was spiked into medium and then included in the extraction procedure (fourth set of bars). Black wedges represent a 1:3 dilution series starting with 50 ng cGAMP. (C) Extract from 10 7 infectious units HIV-1-GFP produced in the presence of cGAS was incubated with or without SVPDE for 1 hour and then added to digitonin permeabilized THP1 cells. IFN in THP1 supernatants was assessed by bioassay. Wedges represent a 1:3 dilution series. (D) HIV-1-GFP produced in the absence or presence of cGAS or in biotin-cGAMP transfected cells was probed by dot blot for biotin (left). The stripped membrane was then re-probed for p24 (right). Wedges represent a 1:10 dilution series starting with 2×10 6 infectious units. FIGS. 5A-5C . Infection of dendritic cells with HIV-1-GFP from cGAS-reconstituted producer cells induces CD86 expression and IFN secretion. Human dendritic cells derived from monocytes from two donors were infected with HIV-1-GFP at the indicated MOIs. After 48 hours, CD86 expression was analyzed by FACS. (A) The percentage of CD86 + cells is shown. (B) The CD86 median fluorescence intensity is shown. (C) Supernatant was tested in the IFN bioassay. (A-C) Average data from duplicate infections for each donor are shown; error bars represent the range. Note that these effects were observed in the absence of Vpx. FIGS. 6A-6E . cGAS lentiviral vector activates dendritic cells. (A) BFP and CD86 expression after infection of monocytes with a lentivirus coding BFP-2A or BFP-2A-cGAS, in presence or absence of Vpx. (B) CD86 expression as in (A) with titrated virus without Vpx and statistical analysis on top dose (paired t test; n=4; ***p<0.001). (C) IP-10 production as in (A) with titrated virus without Vpx and statistical analysis on top dose (paired t test; n=4; **p<0.01 on log-transformed data). (D) BFP and CD86 expression after infection of monocytes with a lentivirus coding BFP-2A or BFP-2A-cGAS, or with VLPs produced in presence of a non-lentiviral plasmid encoding for cGAS (PSTCD-cGAS). (E) CD86 expression and IP-10 production as in (D) (n=5, paired t test for CD86 expression analysis, paired t test on log-transformed data for IP-10; ***p<0.001, **p<0.01, ns=non-significant). FIGS. 7A-7D . cGAS lentiviral vectors activate monocyte and fully differentiated dendritic cells. (A) CD14 and DC-SIGN expression 96 h after transduction of monocytes with a BFP coding vector and a cGAS coding vector in absence of Vpx followed by differentiation in DCs with GM-CSF and IL-4 (n=2). (B) BFP and CD86 expression 48 h post infection of established monocyte-derived dendritic cells with a BFP-2A lentivirus and a BFP-2A-cGAS lentivirus. (C) CD86 expression as in (B) (n=3). (D) Immunoblotting of Gag, cGAS and actin in the producer cells and in the pelleted supernatant used in FIG. 6D . FIGS. 8A-8E . HIV particles transfer an innate signal initiated by cGAS. (A) BFP and CD86 expression after infection of monocytes with a lentivirus produced with the BFP-2A-cGAS vector, Gag/Pol and VSV-G. Cells were infected with complete supernatant or the retentate and filtrate after filtration with a 10 kDa cutoff. A representative experiment out of four is shown. (B) CD86 expression and IP-10 production in dose response infections of monocytes with differentially fractionated supernatants containing VLPs produced from 293FT expressing wild-type cGAS or an inactive cGAS mutant lacking the DNA Binding Domain (ADBD). The volume of each fraction used for infection and the corresponding concentration factor compared to the initial supernatant are indicated (n=3; mean and SEM plotted). (C) Immunoblotting of Gag and cGAS in the fractions obtained by differential centrifugations of the complete supernatant as in (B) (representative of three experiments). (D) Immunoblotting of the exosome markers syntenin-1, CD63, CD81 and CD9 in the fractions obtained by differential centrifugations of the complete supernatant as in (B) (representative of three experiments). (E) CD86 expression analysis of the experiment in (A) (n=4; paired t test; **p<0.01, ns=non-significant). FIGS. 9A-9C . Viral particles package and transfer cGAMP. (A) 293FT cells transfected with a Luciferase reporter plasmid under control of the IFNβ promoter with or without a STING coding plasmid. The cells were either stimulated with titrated amounts of supernatants from cells producing viral particles in presence (cGAS viral particles) or absence (control viral particles) of murine cGAS and supernatants from cells expressing murine cGAS (cGAS no Gag/Pol no VSV-G), stimulated with synthetic cGAMP using lipofectamine or transfected with a plasmid coding for cGAS (cGAS transfection). One representative experiment out of three independent experiments is shown. (B) Type I IFN activity measured after exposure of permeabilized PMA-differentiated THP-1 cells to synthetic 2′-3′-cGAMP (left panel) or to the benzonase-resistant extracts coming from 293FT transfected cells and pelleted viral particles. 293FT cells were transfected with a lentiviral packaging plasmid in presence of cGAS or of the catalytically inactive mutant E225A/D227A (right panel). One representative experiment out of three independent experiments is shown. (C) Immunoblotting of Gag, cGAS and actin in the VLP producer cells used in (A). FIGS. 10A-10F . cGAMP transfer by viral particles is a conserved property of retroviruses. (A) BFP and CD86 expression in DCs after exposure of monocytes to cell-free supernatants of cells transfected with combinations of plasmids expressing Gag/Pol and VSV-G together with plasmids coding cGAS, cGAS E225A/D227A or control. (B) Analysis of CD86 expression and IP-10 production as in (A) (n=6; paired t test for CD86 expression, paired t test on log transformed data for IP-10 production, ****p<0.0001, ***p<0.001, **p<0.01, *0.01
95% according to DC-SIGN staining. CD14 + monocytes were isolated from PBMCs using MACS separation columns and CD14 microbeads (Miltenyi). PBMCs were harvested from CD leukocyte cones (NHS Blood & Transplant, Bristol, UK) using lymphoprep (Alere, UK). HEK293 cells and 293T cells were grown in DMEM medium. THP1 cells, BMDMs and human dendritic cells were grown in RPMI 1640 medium. All media contained 10% FCS and 2 mM glutamine. 100 units/ml penicillin, 100 mg/ml streptomycin and 50 μM 2-mercaptoethanol were additionally added to the RPMI medium used for BMDMs and human dendritic cells. Antibodies, Western Blot and FACS α-hSTING antibody was from Cell Signaling (cat. nb. 3337s; 1:1000) and was used for Western blot with secondary HRP-coupled antibody (GE Healthcare Life Sciences; cat. no. NA934; 1:5000). α-FLAG and α-actin HRP conjugated antibodies were from Sigma (cat. no. A8592, 1:5000 and A3854, 1:10,000). α-CD86 PE (clone IT2.2) and α-CD209 (DC-SIGN) APC (clone eB-h209) were from eBioscience. 1 μg/ml DAPI (Sigma Aldrich) was used to exclude dead cells. FACS data were acquired on Beckman Coulter CyAn or BD Biosciences LSRFortessa cell analyzers. Mice STING-deficient (Mpys −/− ) animals have been described before (Jin et al., 2011 , The Journal of Immunology, 187, 2595-2601) and are on a C57BL/6 background. Femurs and tibias were obtained from humanely killed animals aged 2-3 months and from age and gender matched C57BL/6 wild-type control animals. This work was performed in accordance with the UK Animals (Scientific Procedures) Act 1986 and institutional guidelines for animal care. This work was approved by a project license granted by the UK Home Office (PPL No. 40/3583) and was also approved by the Institutional Animal Ethics Committee Review Board at the University of Oxford. IFN Bioassay Human IFN reporter cells were generated by transducing HEK293 cells with pGreenFire-ISRE derived lentivirus. Single clones were established by limiting dilution and clone 3C11 was selected based on its responsiveness to IFN. For the bioassay, cells were overlaid with cell culture supernatant and after 24 hours luciferase expression was quantified using One-Glo Luciferase Assay System (Promega) according to manufacturer's instructions. The detection limit of the bioassay is 1.6 U/ml hIFNα2 (R&D Systems) as shown in FIG. 2C . RT Q-PCR RNA extraction from cells, reverse transcription and quantitative PCR have been described (Rehwinkel et al., 2013 , EMBO J, 32, 2454-2462). Predeveloped TaqMan assay reagents containing primers and fluorescent probe for human 18S rRNA, IFNβ, IFI-44 and IFIT1 and for murine GAPDH, IFIT1 and IFI-44 were from Applied Biosystems. HIV-1-GFP Production VSV-G pseudotyped HIV-1-GFP was produced in 293T cells transfected with pNL4-3-deltaE-EGFP, pVSV-G and m-cGAS (or m-cGAS-AA) at a ratio of 2:1:2 using FuGene HD (Promega, cat. no. E2311). THOV-G pseudotyped virus was produced with pCAAGS-THOV-G instead of VSV-G and using a plasmid ratio of 1:1:1. Medium was replaced the following day. At this point, DEVD (60 μM; A0835, Sigma) and GW4869 (20 μM; D1692, Sigma) were added in some experiments. After an additional 48 hours, supernatants were filtered (0.22 μm) and, if required, concentrated by centrifugation over a 20% sucrose cushion (64,000 g, 2.5 hours, 4° C.). Viral titres were determined as infectious units/ml by infection of 293T cells with a dilution series of virus stocks, followed by FACS analysis of GFP expression. HIV-1-GFP containing biotin-cGAMP was produced as above in 293T cells transfected with pNL4-3-deltaE-EGFP, pVSV-G and biotin-cGAMP (Biolog, cat. no. 157-001) at a ratio of 2:1:1.6 using FuGene HD. VLPs were produced by transfecting 293T cells with pSIV4+(Vpx deficient), pVSV-G and m-cGAS or m-cGAS-AA at a ratio of 2:1:2. The medium was exchanged the following day. After an additional 48 hours, VLPs were collected and processed as HIV-1-GFP (see above). HIV-1-GFP Infection 10 5 HEK293 were seeded in 24-wells. After 24 hours, virus stocks were added in the presence of polybrene (8 μg/ml). 18 hours later the medium was exchanged. After additional 48 to 72 hours supernatants and cells were harvested for IFN bioassay and FACS analysis or RT Q-PCR analysis, respectively. For the IFNβ promoter reporter assay, cells were additionally transfected with 125 ng p125-F-Luc and with 25 ng pRL-TK using lipofectamine 2000. This was done 6-8 hours prior to infection. Luciferase activity was analysed 24 hours after infection and F-Luc activity was normalized to R-Luc. In some experiments, cells were treated for 1 hour prior to infection with nevirapine (5 μM; cat. no. 4666; NIH AIDS reagent program) or raltegravir (5 μM; cat. no. 11680; NIH AIDS reagent program). Alternatively, virus stocks or cGAS plasmid were pre-treated with DNase I (40 μg/ml; Roche, 11284932001) for 1 hour at 37° C. prior to infection. 4-8×10 5 BMDMs were seeded in 12-wells and, after O/N incubation, were infected in the presence of polybrene (8 μg/ml) by spin-infection (1100 g; 90 min; room temperature). The inoculum was then removed and fresh medium was added. Supernatant and cells were harvested 24 hours later. mIFNα was detected by ELISA as described in Rehwinkel et al., 2013 , EMBO J, 32, 2454-2462. 0.5×10 5 human dendritic cells were seeded in 24-wells and infected for 2 hours in the presence of polybrene (8 μg/ml). The inoculum was washed away and the cells were incubated for 48 hours with fresh medium. The cells were harvested for FACS analysis and the supernatant was tested with the IFN bioassay. Adenovirus Adenovirus was produced in HEK293 cells transfected with m-cGAS or m-cGAS-AA using FuGene HD or in untransfected cells. 2 hours after transfection, cells were infected with AdenoCreGfp virus (cat. no. 1700, Vector Biolabs) at an MOI of 1. Virus was harvested 48 hours later from cells by three cycles of freeze, thaw and sonication. Fresh HEK293 cells were infected for 18 hours. Cells were then washed and provided with new medium. After 48 additional hours, supernatants were harvested for analysis with the IFN bioassay and cells were collected for FACS analysis. Sendai Virus Sendai virus was from LGC Standards (cat. no. VR-907). Cells were infected by addition of Sendai virus to the culture medium. Small Molecule Extractions and THP1 Stimulation The method for small molecule extraction from virions was adapted from Ablasser et al., 2013 , Nature, 498, 380-384. Pelleted virions were resuspended in lysis buffer (1% Triton X-100, 10 mM Tris-HCl, pH 7.4, 1 mM NaCl, 1 mM EDTA and 3 mM MgCl 2 ) and left on ice for 20 min. Lysates were clarified by centrifugation for 10 min at 1000 g at 4° C. To remove nucleic acids, samples were treated for 45 min with 50 U/ml benzonase (Sigma) on ice. Next, proteins were eliminated by two sequential phenol-chloroform extractions followed by a chloroform wash to remove traces of phenol. The extract was filtered using Amicon Ultra 3 kDa centrifugal filters (Millipore, cat. no. UFC500396) and the filtrate was concentrated by centrifugation under vacuum. Samples were resuspended in 20 μl water and stored at −80° C. until further use. 100,000 THP-1 cells treated with 30 ng/ml PMA were seeded in 96-well plates and left overnight. Cells were then washed with medium and overlaid with 25 μl permeabilisation buffer (10 g/ml digitonin, 50 mM Hepes, pH 7.4, 100 mM KCl, 3 mM MgCl 2 , 0.1 mM DTT, 85 mM sucrose, 0.2% BSA, 1 mM ATP and 0.1 mM GTP) containing virion extracts or 2′3′-cGAMP standard (cat. no. C161-005, Biolog) for 30 min at 37° C. Next, cells were washed with medium and 75 μl fresh medium was added. After 24 hours, supernatant was tested in the IFN bioassay. In some experiments, 5 μl extract or 1 μg cGAMP were incubated in 50 mM Tris, pH 8.8, and 10 mM MgCl 2 with or without 0.002 units SVPDE (cat. no. P3243, Sigma) at 37° C. for 1 hour. Treated extracts and cGAMP were then serially diluted in permeabilisation buffer and added to THP1 cells as above. Dot Blot Virus preparations were resuspended in lysis buffer (1% Triton X-100, 10 mM Tris-HCl pH 7.4, 1 mM NaCl, 1 mM EDTA and 3 mM MgCl 2 ) and blotted onto a nylon membrane (Zeta-Probe GT membrane, cat. no. 162-0197, Bio-Rad), which was left to dry and UV cross-linked (UV Stratalinker 2400; 2× Autocross link, 120,000 μJ/cm 2 ). Biotin-cGAMP was detected with streptavidin-HRP (cat. no. 3310-9, Mabtech, 1:1000). HRP was inactivated with 0.2% sodium azide and the absence of residual signal was validated by exposing the membrane for one hour. The membrane was then reprobed with mouse α-p24 (cat. no. 4313, Advanced Bioscience Laboratories, 1:5000) followed by α-mouse HRP (cat. no. NA931VS, GE Healthcare Life Sciences, 1:3000). Example 2 Results To study cGAS function, the inventors sought to manipulate its expression in human monocyte-derived DCs (Dendritic Cells). They generated a lentiviral vector expressing cGAS, produced lentiviral particles and infected monocytes with the cell-free viral supernatant before differentiating them in DCs. At day 4 of differentiation, the majority of differentiated DCs exposed to the cGAS virus expressed CD86 and were therefore activated, although the efficiency of transduction as indicated by expression of the reporter fluorescent protein BFP was low ( FIG. 6A ). In contrast, infection with a lentivirus coding only for BFP efficiently transduced monocytes but did not increase the percentage of activated DCs, as compared to non-virus exposed cells ( FIG. 6A ). This confirmed that the general process of lentiviral vector infection is not sensed by monocytes and DCs and that it could not be responsible for inducing the activation observed in the case of the cGAS lentiviral vector. Importantly, the DCs were fully differentiated, as shown by expression of DC-SIGN and down-regulation of CD14 ( FIG. 7A ). The cGAS lentiviral vector also activated DCs that were fully differentiated prior to infection ( FIG. 7B , FIG. 7C ). This indicated that an activating innate immune signal was present and associated with the apparent process of infection of DCs with a cGAS-expressing lentiviral vector. Efficient expression of a lentivirus-encoded gene in DCs requires the lentiviral protein Vpx which alleviates a constitutive restriction to HIV infection imposed by SAMHD1, thus leading to efficient transduction of the cells by the vector. To check whether expression of cGAS in the target cell was required for activation of the cells, the inventors omitted the Vpx protein from the transduction procedure. In this case, the SAMHD1 restriction is active and prevents efficient transduction, as shown by lack of detection of the reporter fluorescent protein BFP with the control virus ( FIG. 6A , lower panels). Unexpectedly, activation of the DCs by the cGAS lentivirus was conserved without Vpx ( FIGS. 6A, 8B ), suggesting that cGAS expression in the target cells was not required. The activation was not restricted to CD86 expression since the type I interferon-inducible cytokine IP-10 (gene CXCL10) was also produced by DCs ( FIG. 6C ). To confirm this observation and to exclude that a low level of cGAS vector transduction was responsible for the activation, the inventors produced HIV-1 virus-like particles (VLPs) that did not contain a lentiviral genome in cells expressing cGAS from a non-lentiviral plasmid ( FIG. 7D ). The VLP-containing supernatant from cGAS-expressing cells activated DCs to the same extent as the transduction-competent lentiviral vector, as measured by CD86 expression ( FIG. 6D ) and IP-10 production ( FIG. 6E ). Thus, the supernatant from cells that produce viral particles and express cGAS can transmit an innate signal to immune cells. To determine the nature of this signal, the inventors first fractionated viral supernatants over a 10 kDa filter. The retentate efficiently induced CD86 expression and IP-10 production in monocytes, while activity was depleted from the filtrate, indicating that the activity was carried by components larger than 10 kDa ( FIG. 8A , FIG. 8E ). The inventors then performed differential ultracentrifugation, to separate the various types of membrane-enclosed vesicles released by cells in their medium, collectively called extracellular vesicles (EVs), from soluble factors. Cell debris pellet first (2,000 g), followed by large vesicles such as apoptotic blebs (10,000 g), and finally small EVs including exosomes and viruses (100,000 g). Strikingly, the culture supernatant recovered after these ultracentrifugations had almost completely lost ability to activate monocytes ( FIG. 8B ). By contrast, most activity was recovered in the 100,000 g pellet, which contained Gag as well as some exosome-associated proteins, the tetraspanins CD63, CD9, and CD81 and the cytosolic syntenin-1 ( FIG. 8B , FIG. 8C , FIG. 8D ). Some activity was also present in the 10,000 g pellet, which only contained Gag and no exosome markers, whereas the larger cell debris that contained only traces of Gag (not shown) displayed a marginal activity ( FIG. 8B , FIG. 8C , FIG. 8D ). These results show that the innate signal transferred by cGAS-expressing cells to DCs is contained within small EVs, including Gag-containing viral particles, rather than being a diffusible soluble factor. The innate signal that is transmitted by EVs could be mediated by packaging and transfer of the cGAS protein to target cells. The inventors did not favor this hypothesis because they could not detect cGAS protein in the pelleted supernatants ( FIG. 7D ). As an alternative possibility, the second messenger cGAMP could hence transmit the innate signal. cGAMP is a small molecule of 675 Da produced in the cytosol, and could thus be packaged in the viral particles and EVs, since these structures contain cytosol from the producing cells. The inventors reasoned that if cGAMP was present in the cell-derived viral particles, it should activate a type I interferon response in a STING-dependent but cGAS-independent manner. They transfected an interferon reporter construct with or without a STING plasmid in 293FT cells that lack detectable cGAS expression (data not shown). Delivery of synthetic cGAMP with lipofectamine or transfection of cGAS expression plasmid activated the reporter only in the presence of STING, validating the assay ( FIG. 9A , FIG. 9C ). VLPs that were produced from cGAS-expressing cells activated the reporter in the presence of STING, but no activation was detected without STING or when the particles were produced in the absence of cGAS ( FIG. 9A ). Supernatants from cGAS-expressing cells that did not produce VLPs were much less effective at activating the reporter ( FIG. 9A ). Therefore, viral particles can transmit an innate signal from cGAS in produced cells to STING in target cells. To further demonstrate that cGAMP was present in the viral particles, the inventors used a bioassay based on permeabilized THP-1 and an IFN reporter cell line ( FIG. 9B ). They extracted small molecules from viral-producing cells and pelleted VLPs. As expected, cGAMP activity was detected from cells transfected with cGAS, but not in control cells. Strikingly, cGAMP activity was also detected in the pelleted VLPs and this activity was lost when they used the catalytic mutant of cGAS E225A/D227A ( FIG. 9B ). To confirm that the activity measured in the extracts corresponded to cGAMP, the inventors performed mass spectrometry analysis using synthetic cGAMP. They detected the presence of cGAMP in pelleted VLPs. Overall, these data provide strong indications that viral particles package and transfer the second messenger cGAMP. Next, the inventors examined which components were required for transmitting cGAMP. Transmission of cGAMP by the viral particles was abrogated when cGAS E225A/D227A was used, indicating that a functional cGAS protein is required ( FIG. 10A ). VLPs were produced by expressing the viral protein Gag/Pol and the fusogenic viral envelope protein VSV-G. Omitting expression of either Gag/Pol or VSV-G or both decreased the ability of the supernatants to induce CD86 and IP-10 in DCs ( FIGS. 10A, 10B ). Absence of VSV-G decreased most strongly DC activation ( FIGS. 10A, 10B ), indicating that fusogenic extracellular material is the major DC-activating factor. The inventors confirmed that Gag-containing VLPs were still present in the supernatant in the absence of VSV-G, and that VSV-G containing EVs were secreted in the absence of Gag ( FIG. 10C ). Altogether, this indicates that cGAS and fusion-competent EVs including viral particles are required for transmitting cGAMP. Expression of VSV-G by cells leads to production of tubulovesicular structures. To exclude that transmission of cGAMP was a specificity of VSV-G, the inventors produced VLPs carrying the Influenza envelope proteins H1N1 and H5N1 instead of VSV-G. Such particles, which were produced in the presence of cGAS, activated monocytes in all cases ( FIG. 10D , FIG. 11A , FIG. 11E ). The inventors next considered whether cGAMP packaging and transfer to target cells was specific to HIV-1 particles. They produced VLPs from another retrovirus, the gammaretrovirus MLV, and found that they could also transmit cGAMP ( FIG. 10E , FIG. 11B , FIG. 11D ). Finally, they examined whether HIV-1 particles expressing the wild-type CCR5-tropic envelope protein BaL could transfer cGAMP. Indeed, they found that HIV-1 particles produced with cGAS could transmit cGAMP and activate in an innate immune response in target cells ( FIG. 10F , FIG. 11C , FIG. 11E ). Thus, cGAMP packaging and transfer to target cells is a general property of retroviral particles from different origins. Collectively, the present results provide evidence that cGAMP can be transferred between cells by virtue of packaging within viral particles or fusion-competent EVs, defining a new mechanism of innate immune signal transmission ( FIG. 12 ). Spreading of innate responses is generally attributed to the production of cytokines, including interferons. The ensuing innate signals induce the production of effector molecules. Interestingly, some antiviral effectors can be packaged into viral particles and EVs, such as APOBEC3G, but effectors do not directly induce an innate immune response in the target cells. cGAMP has the ability to diffuse between cells that are physically connected by gap junctions. Viral transfer of cGAMP does not require a direct contact between the cells, which may allow transmission of an innate signaling molecule within the organism or during transmission between hosts. This process could maximize the rapid induction of effector responses in target cells. Interestingly, immunostimulatory cyclic dinucleotides that are produced by bacteria can be delivered into the target cell and induce an innate immune signal, providing an appealing parallel with viral-mediated transfer of cGAMP. The present results additionally indicate that non-viral cell-derived EVs that could be exosomes can also transmit cGAMP to some extent. Consistent with this finding, EVs can transmit cellular RNA between cells. However, transmission of cGAMP is of low efficiency in the absence of a fusogenic viral envelope protein. The inventors speculate that the step of membrane fusion with the target cell membrane is limiting in the case of EVs from non-infected cells. Nevertheless, in addition to its function as a viral sensor, cGAS appears to contribute to setting the tonic level of interferon-induced genes in uninfected mice, which plays a crucial role in determining subsequent susceptibility to infection. Although it is not yet known whether this function of cGAS requires cGAMP synthesis, transmission of cGAMP by host EVs might contribute to set the tonic interferon response. The inventors demonstrate that the vectorization of cGAMP by VLP of the present invention is far more efficient than 2′3′-cGAMP complexed with lipofectamine (i.e., MLV Gag and HIV Gag VLPs being approximately 1,000 fold more efficient) and than 2′3′-cGAMP in inducing dendritic cell maturation (i.e., MLV Gag and HIV Gag VLPs being approximately 10,000 fold more efficient) ( FIG. 14 ). The inventors propose that packaging of cGAMP within viral particles can be interpreted as an immune tagging process. This may allow infected cells to further signify progeny viruses as non-self, or dangerous, in order to alert subsequent target cells. It is tempting to speculate that other signaling molecules are also packaged and disseminated by viral particles. Finally, cGAMP packaging by expressing its synthesizing enzyme in cells producing viral particles provides an attractive strategy to vectorize immunogenic cyclic dinucleotides for therapeutics and vaccines. Materials and Methods Cells 293FT and HL-116 cells were cultured as previously described (Lahaye et al., 2013, Immunity, 39, 1132-1142). Monocytes were isolated from peripheral adult human blood as previously described (Lahaye et al., supra). Monocytes were cultured and differentiated into dendritic cells in RPMI medium with GlutaMAX, 10% FBS (Biowest or GIBCO), Penicillin-Streptomycin (GIBCO), Gentamicin (50 mg/ml, GIBCO), and HEPES (GIBCO) in the presence of recombinant human GM-CSF (Miltenyi) at 10 ng/ml and IL-4 (Miltenyi) at 50 ng/ml. THP-1 were cultured in RPMI medium with GlutaMAX, 10% FBS (GIBCO), and Penicillin-Streptomycin (GIBCO). Constructs Human cGAS WT open reading frame was amplified by PCR from cDNA prepared from monocyte-derived dendritic cells. Murine cGAS WT open reading frame was amplified by PCR from cDNA prepared from C57BL6 murine bone-marrow derived dendritic cells. Human cGAS E225A/D227A mutant was obtained by overlapping PCR mutagenesis. ntcGAS was obtained by overlapping PCR mutagenesis in order to generate a cGAS variant that is non-targetable by the shRNAs previously described (Lahaye et al., supra). mTagBFP2 (Subach et al., 2011, PLoS One, 6, e28674) sequence was generated synthetically (Invitrogen). The plasmids pSIV3+, psPAX2, pCMV-VSV-G and pTRIP-CMV were previously described (Satoh et al., 2013 , Methods Mol Biol, 960, 401-409). BFP-2A, BFP-2A-FLAG-ntcGAS, BFP2AFLAG-cGAS E225A/D227A, Puro-2A were cloned in pTRIP-CMV. Non-lentiviral vectors were based on the mammalian expression plasmid pcDNA3.1-Hygro(+) (Invitrogen). Mouse WT, human WT cGAS, human cGAS E225A/D227A, PSTCD-cGAS and PSTCD-cGAS ADBD were cloned in pcDNA3.1-Hygro(+) by PCR. Propionibacterium shermanii transcarboxylase domain (PSTCD) is a streptavidin-binding protein (Fukata et al., 2013 , J Cell Biol, 202, 145-161). PSTCD-cGAS ΔDBD was generated by deleting amino acid regions K173-1220 and H390-C405 by overlapping PCR. The human isoform of cGAS was used in all experiments except noted otherwise. Human STING open reading frame was cloned by PCR from the IMAGE clone 5762441. This clone encodes a histidine residue at position 232, which was mutated into an arginine residue by overlapping PCR mutagenesis (Diner et al., 2013 , Cell Reports, 3, 355-1361). STING R232 was cloned in pMSCVhygro (Addgene) by PCR. In all final constructs, the entire DNA fragments originating from the PCR and encompassing the restriction sites used for cloning were fully verified by sequencing. IFNβ-pGL3 plasmid was obtained from the lab of Olivier Schwartz, Pasteur Institute. The Influenza envelope plasmids encoding for H1, H5 and N1 were obtained from the lab of Adolfo Garcia-Sastre, Mount Sinai Medical Center. MLV Gag/Pol was expressed from pCL-10A1 (Naviaux et al., 1996 , J Virol, 70, 5701-5705). Replication competent CCR5-tropic R5GFP construct was NL4-3/BaL env, Δnef, enconding GFP in nef, previously described (Lahaye et al., supra). Viruses Viral particles were produced as previously described from 293FT cells (Lahaye et al., supra). Lentiviral particles and virus-like particles were produced by transfecting 1 μg of psPAX2 and 0.4 μg of pCMV-VSV-G together with 1.6 μg of a mammalian expression plasmid or lentiviral vector plasmid per well of 6-well plate. For CCR5 tropic NL4-3/BaL env virus 1.6 μg of pcDNA3.1-Hygro(+)-ms cGAS plasmid was co-transfected with 1.4 μg of R5GFP plasmid. For Influenza psuedotyped VLPs 1 μg of pcDNA3.1-Hygro(+)-ms cGAS plasmid was co-transfected with 1 μg of psPAX2 and 0.5 μg of either H1 or H5 and 0.5 μg of N1 encoding plasmids. For MLV viral particles 1.6 μg of pTRIP-CMV-BFP-2A or pTRIP-CMV-BFP2A-FLAG-ntcGAS were mixed with 1 μg of pCL-10A1 and 0.4 μg of pCMV-VSV-G. When psPAX2 and/or pCMV-VSV-G were omitted the same amount of DNA was substituted by pcDNA3.1-Hygro(+). Virus-containing cell supernatants were systematically filtrated over 0.45 μM filters. For cGAMP OVA VLPs and cGAMP VLPs used in FIG. 14 , the viral particles were concentrated and purified as follows. 34 ml of crude supernatant coming from 293FT were loaded in Ultra-Clear Centrifuge tubes (Beckman Coulter) on top of 6 ml of a sucrose (Sigma) cushion (20% dissolved in PBS) and ultracentrifuged at 100,000 g in an SW32 rotor (Beckman Coulter). The recovered viral pellet was resuspended in 13 ml of PBS and transferred in new Ultra-Clear Centrifuge tubes and ultracentrifuged at 100,000 g in an SW41 rotor (Beckman Coulter). The recovered pellet was then resuspended in 750 μl of PBS for cGAMP OVA VLPs or in 1350 μl of PBS for cGAMP VLPs. Three aliquots of 50 μl of each prep were transferred into a separate tube for cGAMP extraction, monocytes infection and p24/p27 ELISA, respectively. All the aliquots were then frozen at −80° C. until further use. Infections 50,000 freshly isolated monocytes or day 4 differentiated DCs were seeded in 96-well U bottom plates and infected in a final volume of 200 μl with Protamine (Sigma) at 81 g/ml in presence of human recombinant GM-CSF (Miltenyi) at 10 ng/ml and IL-4 (Miltenyi) at 50 ng/ml. Infections with Influenza envelope pseudotyped VLPs and HIV1 NL4-3/BaL env viruses were performed with an additional spinoculation step at 1200 g, 25° C. for 2 hours. When indicated, Vpx was delivered by adding 50 μl of SlVmac VLPs produced as previously described (Lahaye et al., supra). AZT (Sigma) was added at 25 μM. For the Luciferase assay, VLPs produced in presence or absence of pcDNA3.1-Hygro(+)-ms cGAS were used to infect 293FT in a final volume of 2.5 ml with Protamine at 81 μg/ml. Western Blotting 293FT cells were detached with PBS and cell pellets were lysed in Sample Buffer (2% SDS, 10% glycerol, 0.05M Tris-HCl pH 6.8, 0.025% bromophenol blue, 0.05M DTT). Virus supernatants were filtered at 0.45 μm and centrifuged at 16,000 g for 2 hours at 4° C. Unless noted otherwise, virus pellets were lysed in 65 μl of sample buffer. Cellular and viral protein lysates were resolved on 4%-20% SDS-PAGE gels (Bio-Rad) and transferred on nitrocellulose membrane (Bio-Rad). Proteins were blotted with antibodies as follows: mouse monoclonal anti-Gag (clone 183-H12-5C-produced in-house), mouse monoclonal anti-VSV tag (clone P5D4—produced in-house), rabbit polyclonal anti-MB21D1 (Sigma), mouse monoclonal anti-Actin (clone C4—Millipore), supernatant from R187 hybridoma for MLV Gag (Chesebro et al., 1983 , Virology, 127, 134-148) (provided by Marc Sitbon and Jean-Luc Battini), mouse monoclonal anti-CD9 (clone MM2/57—Millipore), mouse monoclonal anti-CD81 (clone B-11—Santa Cruz Biotechnology), mouse monoclonal anti-CD63 (clone H5C6—BD Bioscience), rabbit polyclonal anti-Syntenin-1 (kindly provided by Pascale Zimmerman) (Zimmermann et al., 2001 , Molecular Biology of the Cell, 12, 339-350) and Streptavidin-HRP (Pierce) in the case of PSTCD-cGAS proteins. ECL signal was recorded on the ChemiDoc XRS Imager (Bio-Rad). Data was analyzed with Image Lab (Bio-Rad). Luciferase Assay 293FT cells were plated in a 24-well plate. The next day, cells were transfected with 300 ng of total DNA comprising IFNβ-pGL3 and the empty vector pTRIP-CMV-Puro-2A or pMSCVhygro-STING R232 with TransIT-293 (Mirus). The next day, medium was removed and replaced with 2.5 ml of crude supernatant coming from 293FT-producer cells. 3′3′ cGAMP (InvivoGen) was delivered with Lipofectamine 2000 (Invitrogen) transfection (1 μg 3′3′cGAMP:1 Lipofectamine 2000) in a final volume of 500 μl. After 24 hours cells were washed with PBS and lysed with Passive Lysis Buffer (Promega) and 10 μl of the lysate were used to perform the Luciferase assay. Luciferase activity was measured using Luciferase Assay Reagent (Promega). Luminescence was acquired on a FLUOstar OPTIMA microplate reader (BMG labtech). cGAMP Extraction and Bioassay The assay was adapted from previously described protocols (Woodward et al., 2010 , Science, 328, 1703-1705; Ablasser et al., 2013 , Nature, 497, 380-384; Wu et al., 2012, Science, 339, 826-830). 293FT cells and supernatants were recovered as described for Western blotting. After centrifugation, cells and viral pellets were lysed in lysis buffer (1 mM NaCl, 3 mM MgCl 2 , 1 mM EDTA, 10 mM Tris-HCl pH7.4, 1% Triton X-100) for 20 minutes at 4° C. The cells and viral lysates were centrifuged at 1000 g for 10 min and the supernatant was treated with 50U/ml of Benzonase (Sigma) for 45 minutes at 4° C. The suspension was then extracted using Phenol:Chloroform:Isoamyl alcohol (25:24:1, v/v—Sigma) for two rounds, and the recovered aqueous phase was then washed with Chloroform (VWR Chemicals). The remaining aqueous phase was loaded on an Amicon 3KDa cutoff column (Millipore) and centrifuged at 14000 g for 30 minutes. The eluted solution was then subjected to speed vacuum in Savant DNA Speed Vac DNA 110 at 43° C. for 2 hours. For cGAMP OVA VLPs and cGAMP VLPs used in FIG. 14 , to a 50 μl aliquot 50 μl of DNAse/RNAse Free Water (GIBCO) were added; the obtained 100 μl were then lysed with 400 μl of methanol (VWR Chemicals) in order to obtain an 80/20 (v/v) mix of MeOH/H 2 O. The lysates were subjected to 5 cycles of freezing and thawing, and centrifuged at 16,000 g at 4° C. for 20 min. The recovered supernatants were then subjected to speed vacuum in Savant DNA Speed Vac DNA 110 at 43° C. for 2.5 hours or at 65° C. for 2.5 hours. As an internal control for the extraction process, known quantities of 2′3′-cGAMP were spiked in an 80/20 (v/v) mix of MeOH/H 2 O and extracted as the viral preps, omitting the freeze and thaw steps. The pellets were resuspended in 25 μl (Phenol:Chloroform:Isoamyl alcohol extraction) or 30 μl (methanol/water extraction) of RNAse-DNAse free water (GIBCO) and used on THP-1. 24 hours prior to the assay, 100,000 THP-1 cells were re-suspended in fresh medium with PMA (Sigma) at 30 ng/ml and seeded in 96-well plate flat bottom. PMA was then washed and THP-1 cells were treated with the resuspended samples during permeabilization with a buffer containing 50 mM HEPES (GIBCO), 100 mM KCl, 3 mM MgCl 2 , 0.1 mM DTT, 85 mM sucrose (Sigma), 1 mM ATP (Sigma), 1 mM GTP (Sigma), 0.2% BSA (Euromedex), and 0.001% Digitonin (Calbiochem) for 30 minutes at 37° C., 5% CO 2 atmosphere. At the same time permeabilized THP-1 cells were treated with synthetic 2′3′ cGAMP (InvivoGen). The buffer was then washed and fresh medium was added on the cells and incubated overnight. For samples extracted with MeOH/H 2 O, 50U/ml of benzonase were added during the initial stimulation phase. The supernatant was then transferred on HL-116 cells to measure interferon activity as described (Lahaye et al., supra). Filtration 293FT cells were transfected with 1.6 μg of pTRIP-CMV-BFP-2A-FLAG-ntcGAS, 1 μg of psPAX2 and 0.4 μg of pCMV-VSV-G and treated as previously described for virus production. The supernatant was then recovered and centrifuged on an Amicon 10KDa cutoff tube (Millipore) for 30 minutes at 4,000 g at 4° C. The retentate was resuspended in previously described DC media. The resuspended retentate and the filtrated fraction were then used to treat monocytes as previously described. Fractionation RPMI with GlutaMAX medium containing 10% FBS and Penicillin-Streptomycin was depleted from bovine EVs by an overnight centrifugation at 100000 g and then filtered at 0.22 μm. 293FT were transfected as described for viruses. 12 hours after transfection, medium was replaced with fresh EV-depleted medium. 30 hours later, the supernatant was recovered and filtered at 0.45 m. Vesicles were isolated from conditioned medium by sequential untracentrifugation steps: 20 minutes at 2,000 g (bench-top centrifuge); 25 minutes at 9,000 rpm (ultracentrifuge XL-100K Beckman with SW55Ti rotor, k_factor=1,759.27, 10,000 g fraction); 1 hour at 30,000 rpm (ultracentrifuge XL-100K Beckman with SW55Ti rotor, k_factor=169.44, 100,000 g fraction). Each pellet was suspended in either 50 μl of PBS (Western blotting) or 600 μl of EV depleted media (infection of monocytes). The remaining supernatant of the 100,000 g fraction was used only for infection of monocytes. Flow Cytometry Cell surface staining was performed in PBS, 1% BSA (Euromedex), 1 mM EDTA (GIBCO). The antibodies used were anti-human CD86 PE (clone IT2.2—eBioscience), anti-human CD14 FITC (clone 61D3—eBioscience) and anti-human DC SIGN PE (clone 120507—R&D Systems). Cells were stained for 15 minutes at 4° C., washed for two times and fixed in 1% paraformaldehyde (Electron Microscopy Sciences). Data was acquired on a FACSVerse (BD) or an Accuri C6 (BD) and analyzed in FlowJo. IP-10 Protein Quantification IP-10 concentration was measured on pure or 10-fold dilutions (100,000 g fraction, Influenza pseudotyped viral particles, NL4-3/BaL env virus) of supernatants from treated monocytes. IP-10 concentration was measured with a Human IP-10 cytometric assay (BD) according to the manufacturer's protocol. Data was acquired on a BD FACSVerse (BD) and analyzed in FCAP Array (BD). Statistics Statistical analyses were performed in Prism (GraphPad). Mass Spectrometry Extracts obtained after cGAMP extraction procedure were diluted (1/1000, 1/100 or 1/10) in solution A (2% (v/v) acetonitrile/water, 0.1% (v/v) formic acid) and analyzed (1 μL) using an actively split capillary HPLC system (Ultimate 3000, Dionex, Germering, Germany) connected to a QSTAR Elite quadrupole time-of-flight (Q-TOF) mass spectrometer (Applied Biosystems/MDS SCIEX). Sample separation was achieved on an analytical C18 column (75 am id×150 mm long, packed with 3 am particles with 100 Å pore size, C18 PepMap™, Dionex S.A.) using a 30 min isocratic elution (5% (v/v) B, 95% (v/v) A, with mobile phase B, 80% (v/v) acetonitrile/water, 0.085% (v/v) formic acid) at 200 nL/min. Data acquisition was performed using the Analyst QS Software (2.0), set for the positive-ion mode with an electrospray (ESI) voltage of 2.2 kV. TOF-MS survey scan was acquired for 1 s over a mass range of 300-800 m/z. Then a product acquisition method was used to acquire product ion scans of ion m/z 675.1 at 40 eV collision energy (CE) per cycle of 2 s over a mass range of 50-680 m/z and three product ion scans in pseudo selected reaction monitoring (pseudo-SRM) mode of ion m/z 675.1 at 30 eV CE per cycle of 1 s over mass range 520-530 m/z, at 60 eV CE per cycle of 1 s over mass range 120-170 m/z and at 40 eV CE per cycle of 1 s over mass range 460-490 m/z. Example 3 Results The inventors sought to determine whether transfer of cGAMP by viral particles would occur at physiologically relevant levels of cGAS expression. HeLa cells express the cGAS protein. HeLa cells did not contain detectable amounts of intracellular cGAMP at steady-state, but it was detected after DNA stimulation. Disruption of the cGAS gene by CRISPR/Cas9 in HeLa abolished cGAMP production after DNA stimulation. Next, the inventors harvested the pelletable extracellular material of control HeLa, DNA-stimulated HeLa or HeLa transfected with VLP-coding plasmids (which also provide a DNA stimulus). cGAMP was detected in the material of all DNA-stimulated HeLa, consistent with it being packaged in extracellular vesicles (EVs) and viral particles ( FIG. 13A ). However, only HeLa-derived VLPs induced IP-10 production in PMA-treated THP-1 cells, and not EVs from control HeLa or DNA-stimulated HeLa ( FIG. 13B ). To ascertain that cGAMP was transferred, the inventors tested the material in the STING Luciferase reporter assay. HeLa-derived VLPs, but not EVs from DNA-stimulated HeLa, activated the interferon promoter in a STING-dependent manner ( FIG. 13C ). Overall, these data demonstrate that viral particles and EVs package cGAMP produced by endogenous cGAS, but only viral material can efficiently transfer the second messenger cGAMP. Methods HeLa Transfection 0.8 million HeLa cells per well were seeded in a 6 well plate and transfected the same day. Transfection was performed with 7.5 μl of Lipofectamine 2000 (Invitrogen) and 4 μg of DNA total. In the case of Empty Vector transfections, 4 μg of pcDNA3.1-Hygro(+) were delivered. In the case of VLPs, 3.5 μg of psPAX2 and 0.5 μg of pCMV-VSV-G were transfected. In the case of HIVGFP, 3.5 μg of HIVGFP env-nef- and 0.5 μg of pCMV-VSV-G were transfected. The medium was changed after 14-16 hours. The supernatant was then harvested after 28-30 hours and systematically filtered at 0.45 μm. For cGAMP extraction and THP-1 stimulation the supernatant was first centrifuged at 2000 g for 20 minutes at 4° C., and then 30 ml were loaded in Ultra-Clear Centrifuge tubes (Beckman Coulter) and ultracentrifuged at 100000 g in an SW32 rotor (Beckman Coulter). For the IFN-βLuciferase reporter assay the 2000 g centrifugation was skipped. The obtained ultracentrifuged pellets were resuspended in RPMI 10% FBS (GIBCO), PenStrep to treat THP-1, in DMEM 10% FBS (GIBCO), PenStrep for the IFN-β Luciferase reporter assay, and in 500 μl of lysis buffer (1 mM NaCl, 3 mM MgCl 2 , 1 mM EDTA, 10 mM Tris-HCl pH7.4, 1% Triton X-100) for cGAMP extraction. Cells were recovered by trypsinization, pelleted, washed with PBS, resuspended in lysis buffer for cGAMP extraction and then frozen at −80° C. THP-1 Stimulation 100,000 THP-1 cells were seeded the day prior to stimulation in a 96 well plate flat bottom in fresh medium containing PMA (SIGMA) at 30 ng/ml. Before stimulation the medium was replaced with fresh medium and the cells were then treated with the re-suspended ultracentrifuged material in presence of 81a/ml of Protamine (SIGMA). 48 hours after stimulation the supernatant was collected and stored at 4° C. until IP-10 quantification. IP-10 Protein Quantification IP-10 concentration was measured on pure or 10-fold dilutions of supernatants from treated THP-1. IP-10 concentration was measured with a Human IP-10 cytometric assay (BD) according to the manufacturer's protocol. Data was acquired on a BD FACSVerse (BD) and analyzed in FCAP Array (BD). Luciferase Assay 45,000 293FT cells were plated in a 24-well plate. The next day, cells were transfected with 500 ng of total DNA comprising 200 ng of IFNβ-pGL3 and 300 ng of the empty vector pMSCV-hygro or pMSCV-hygro-STING R232 with TransIT-293 (Mirus). For RIG-I N228 transfections, 150 ng of pCAGGS-FlagRIGIN228 were co-transfected with 150 ng of the empty or STING expressing vector. The next day, medium was removed and replaced with 380 μl of the re-suspended pelleted material in presence of 81 μg/ml of Protamine (SIGMA). In the case of HIVGFP env-nef-(G) pellets, 293FT cells were treated with 251 μM AZT (SIGMA) and 10 μM Nevirapine (SIGMA). 2′3′ cGAMP (InvivoGen) was delivered with Lipofectamine 2000 (Invitrogen) transfection (1 μg 2′3′ cGAMP:1 μl Lipofectamine 2000) in a final volume of 380 μl. After 24 hours cells were washed with PBS and lysed in Passive Lysis Buffer (Promega). 10 μl of the lysate were used to perform the Luciferase assay. Luciferase activity was measured using Luciferase Assay Reagent (Promega). Luminescence was acquired on a FLUOstar OPTIMA microplate reader (BMG Labtech). cGAMP Extraction and Bioassay Cells and supernatants were recovered as described. The lysates were subjected to 5 cycles of freeze thawing. The lysates were then boiled at 95° C., cooled down in ice and centrifuged in a benchtop centrifuge at 16000 g for 20 minutes at 4° C. The supernatant was then recovered and treated with 50U/ml of Benzonase (Sigma) for 45 minutes at 4° C. The suspension was then extracted using Phenol:Chloroform:Isoamyl alcohol (25:24:1, v/v—Sigma) for two rounds, and the recovered aqueous phase was then washed with Chloroform (VWR Chemicals). The remaining aqueous phase was loaded on an Amicon 3KDa cutoff column (Millipore) and centrifuged at 14000 g for 30 minutes. The eluted solution was then subjected to speed vacuum in Savant DNA Speed Vac DNA 110 at 65° C. for 2 hours. The pellet was resuspended in RNAse-DNAse free water (GIBCO) and used on THP-1. 24 hours prior to the assay, 100,000 THP-1 cells were re-suspended in fresh medium with PMA (Sigma) at 30 ng/ml and seeded in 96-well plate flat bottom. PMA was then washed and THP-1 cells were treated with the resuspended samples during permeabilization with a buffer containing 50 mM HEPES (GIBCO), 100 mM KCl, 3 mM MgCl 2 , 0.1 mM DTT, 85 mM sucrose (Sigma), 1 mM ATP (Sigma), 1 mM GTP (Sigma), 0.2% BSA (Euromedex), and 0.001% Digitonin (Calbiochem) for 30 minutes at 37° C., 5% CO 2 atmosphere. At the same time permeabilized THP-1 cells were treated with synthetic 2′3′ cGAMP (InvivoGen). The buffer was then washed and fresh medium was added on the cells and incubated overnight. The supernatant was then transferred on HL-116 cells to measure interferon activity as described. Quantitative Bioassay for IFNs Supernatants from THP-1 stimulated cells were assayed for IFN activity with the HL116 cell line, which carries a luciferase reporter controlled by the IFN-inducible 6-16 promoter, as previously described (Uze′ et al., 1994). In brief, the reporter cells were exposed to cell culture supernatants for 5 hr and assayed for luciferase activities (Promega), which were then translated to IFN activities by using a standard curve generated from a serial dilution of human IFNalpha-2a (ImmunoTools). Example 4 Results To test the activity of cGAMP-VLPs to control tumor growth in a prophylactic vaccination setting, the inventors treated mice with Ova-cGAMP-VLPs, control cGAMP-VLPs, Ova protein+cGAMP or Ova protein+CpG ( FIGS. 15A , B). Day 11 post-immunization, Ova-specific CD8+ T cells were detected with Ova-cGAMP-VLPs but not with control VLPs ( FIG. 15C ). An Ova-expressing tumor was grafted at day 14. On Day 25, the presence of the Ova-specific CD8+ T cell response was confirmed and increased ( FIG. 15D ). In untreated mice and mice vaccinated with control cGAMP-VLPs or Ova protein+cGAMP, tumor growth was observed ( FIG. 15E ). In contrast, Ova-cGAMP-VLP and Ova protein+CpG treated mice were completely protected from tumor growth. Thus, this establishes that Ova-cGAMP-VLPs are functional in vivo as a prophylactic vaccine to induce CD8+ T cell responses and prevent tumor growth. Next, to test the activity of cGAMPs as a therapeutic immunomodulator in the absence of tumor antigens, the inventors grafted an Ova-expressing tumor in mice and at day 12 treated intratumorally with cGAMP-VLPs or control ( FIGS. 15F, 15G ). In cGAMP-VLPs treated mice, an Ova-specific CD8+ T cell response was detected, but not in control treated mice ( FIG. 15H ). This establishes that cGAMP-VLPs can provide a therapeutic immunomodulatory signal to induce a tumor-specific CD8+ T cell response. Methods Mice and Vaccination 5/6-week-old female C57BL/6J mice were purchased from Charles River France. The care and use of animals used here was strictly applying European and National Regulation for the Protection of Vertebrate Animals used for Experimental and other Scientific Purposes in force (facility license #C75-05-18). It complies also with internationally established principles of replacement, reduction and refinement in accordance with Guide for the Care and Use of Laboratory Animals (NRC 2011). Mice were injected either subcutaneously (s.c.) in the footpads or intratumorally (i.t.). Quantification of CD8 + T Cell Responses 10 days after injection of VLPs, blood samples were collected by retro-orbital puncture and CD8+ Ova-specific T cell responses were measured using tetramer analysis and quantification of IFN-g producing cells by ELISPOT. Total blood cells were stained with PE-conjugated H-2Kb/SIINFEKL tetramer (Beckman Coulter), anti-CD8 and anti-TCR antibodies (BD Biosciences), followed by red blood cell lysis to quantify OVA-specific CD8 + T cells. Cells were analyzed using a standard LSR-II flow cytometer (BD Biosciences) and the FACS data were analyzed using FlowJo software. The tetramer + cells were gated on TCR + CD8 + cells. At the same time, IFNγ-producing OVA-specific CD4 + or CD8 + T cells were measured by ELISPOT on PBMC after red blood cell lysis. Briefly, microplates (Multiscreen HTS IP, Millipore) were coated with anti-murine IFNγ antibody (Diaclone). PBMC (0.2×10 6 /well) were cultured overnight in the presence of either control medium or the 257-264 (SIINFEKL) class I-restricted OVA peptide (10 μM) (Polypeptide Group, Strasbourg, France) in complete medium (RPMI-GlutaMAX, 10% fetal calf serum, antibiotics, R-mercaptoethanol). The detection was performed with a biotinylated anti-IFNγ (matched pairs, Diaclone) followed by streptavidin-alkaline phosphatase (Mabtech) and revealed using the appropriate substrate (Bio-Rad). Spots were counted using an ELISPOT Reader System ELR02 (AID, Germany) and results were expressed as the number of cytokine-producing cells per 0.2×10 6 PBMC. Quantification of OVA-Specific Antibody Responses 12 days after immunization, sera were collected by retro-orbital puncture and OVA-specific immunoglobulins were measured by standard ELISA. Briefly, Maxisorp 96-well plates were coated at 4° C. with OVA (10 μg/ml) in carbonate/bicarbonate buffer. After blocking with PBS-5% milk for 2 h, serially diluted sera were added for 2 h at room temperature. After extensive washing, alkaline phosphatase-conjugated anti-mouse IgG, IgG1 or IgG2b (Jackson ImmunoResearch) was added to each well and plates were incubated 1 h at room temperature. After extensive washing, alkaline phosphatase activity was measured adding the CDP-Star® Ready-to-Use substrate (Applied Biosystems). The microplates were read using a Centro LB 960 luminometer (Berthold) and sample sera were compared to a positive standard curve to express the results in arbitrary units (AU). In Vivo Tumor Assays 0.5×10 6 B16F10-OVA cells were administered subcutaneously into the shaved flank of the mice. Tumor growth was measured twice a week using a caliper to determine the tumor size, calculated as (length×width 2 )/2). Mice were sacrificed when tumor reached 2 cm 3 . For tumor prevention experiments, mice were injected with VLPs (Ova-cGAMP-VLPs: estimated 11 ng cGAMP and 10 ng MLV p30 per injection) and tumor cells were injected s.c. 14 days later. For tumor therapeutic setting, tumor cells were injected s.c. and when tumors reached 30-100 mm 3 mice were injected i.t. with VLPs (cGAMP-VLPs: estimated 33 ng cGAMP and 43 ng HIV p24 per injection). EMBODIMENTS OF THE INVENTION Embodiment 1 A virus-like particle comprising a lipoprotein envelope including a viral fusogenic glycoprotein, wherein said virus-like particle contains cyclic dinucleotides packaged into said virus-like particle. Embodiment 2 The virus-like particle according to embodiment 1, wherein the virus-like particle further comprises a capsid from retroviridae. Embodiment 3 The virus-like particle according to any one of embodiments 1-2, wherein the viral fusogenic glycoprotein is a glycoprotein from retroviridae (including lentivirus and retrovirus), herpesviridae, poxviridae, hepadnaviridae, flaviviridae, togaviridae, coronaviridae, hepatitis D virus, orthomyxoviridae, paramyxoviridae, filoviridae, rhabdoviridae, bunyaviridae, or orthopoxiviridae (e.g., variola), preferably from orthomyxovirus, retroviruses, or rhabdovirus. Embodiment 4 The virus-like particle according to any one of embodiments 1-3, wherein the viral fusogenic glycoprotein is a glycoprotein from HIV (Human Immunodeficiency Virus) including HIV-1 and HIV-2, Influenza including Influenza A (e.g., subtypes H5N1 and H1N1) and Influenza B, thogotovirus, or VSV (Vesicular Stomatitis Virus). Embodiment 5 The virus-like particle according to any one of embodiments 2-4, wherein the retroviral capsid is from retroviridae, preferably lentivirus and retrovirus. Embodiment 6 The virus-like particle according to any one of embodiments 2-5, wherein the retroviral capsid is from HIV or MLV (Murine Leukemia Virus). Embodiment 7 The virus-like particle according to any one of embodiments 1-6, wherein the cyclic dinucleotides are selected from the group consisting of cyclic di-adenosine monophosphate (c-di-AMP), cyclic di-guanosine monophosphate (c-di-GMP), and cyclic guanosine monophosphate-adenosine monophosphate (cGAMP). Embodiment 8 The virus-like particle according to any one of embodiments 1-7, wherein the cyclic dinucleotides are cGAMP (2′-3′-cyclic GMP-AMP). Embodiment 9 The virus-like particle according to any one of embodiments 1-8, wherein it further comprises an antigen or any other protein or nucleic acid of interest. Embodiment 10 The virus-like particle according to any one of embodiments 1-9 as a drug. Embodiment 11 The virus-like particle according to any one of embodiments 1-9 as a vaccine adjuvant. Embodiment 12 A pharmaceutical, vaccine or veterinary composition comprising a virus-like particle according to any one of embodiments 1-9 and a pharmaceutically acceptable carrier. Embodiment 13 The pharmaceutical, vaccine or veterinary composition according to embodiment 12, wherein it further comprises an antigen or a therapeutic active agent. Embodiment 14 A method for inducing or enhancing an immune response in a subject comprising administering a virus-like particle according to any one of embodiments 1-9 or a composition according to embodiment 12 or 13. Embodiment 15 A method for preventing or treating an infectious disease or a cancer in a subject comprising administering a virus-like particle according to any one of embodiments 1-9 or a composition according to embodiment 12 or 13. Embodiment 16 An expression vector or a combination of expression vectors, comprising a sequence encoding a cyclic dinucleotide synthase and either a sequence encoding a viral fusogenic glycoprotein or a sequence encoding a retroviridae capsid protein, or both. Embodiment 17 The expression vector or combination thereof according to embodiment 16, wherein the cyclic dinucleotide synthase is selected from the group consisting of the diadenylate cyclase, diguanylate cyclase and the cyclic GMP-AMP synthase. Embodiment 18 The expression vector or combination thereof according to embodiment 16 or 17, wherein the cyclic dinucleotide synthase is cGAS (Cyclic GMP-AMP synthase). Embodiment 19 The expression vector or combination thereof according to any one of embodiments 16-18, wherein the expression vector comprises both a sequence encoding a viral fusogenic glycoprotein and a sequence encoding a retroviridae capsid protein. Embodiment 20 The expression vector or combination thereof according to any one of embodiments 16-19, wherein the expression vector further comprises a sequence encoding an antigen or any other protein or nucleic acid of interest. Embodiment 21 The expression vector or combination thereof according to any one of embodiments 16-20, wherein the expression vector is a plasmid, a baculovirus vector or a viral vector. Embodiment 22 The expression vector or combination thereof according to embodiment 21, wherein the viral vector is selected from the group consisting of adenoviral vector, adeno-associated virus based vector, and lentiviral vector. Embodiment 23 The expression vector or combination thereof according to any one of embodiments 16-22 as a drug or a vaccine adjuvant. Embodiment 24 A pharmaceutical, vaccine or veterinary composition comprising an expression vector or combination thereof according to any one of embodiments 16-22 and a pharmaceutically acceptable carrier. Embodiment 25 A method for inducing or enhancing an immune response in a subject comprising administering an expression vector according to any one of embodiments 16-22 or a composition according to claim 24 . Embodiment 26 A method for preventing or treating an infectious disease or a cancer in a subject comprising administering an expression vector according to any one according to embodiments 16-22 or a composition according to embodiment 24. Embodiment 27 A recombinant eukaryotic host cell comprising a sequence encoding a cyclic dinucleotide synthase and a sequence encoding a viral fusogenic glycoprotein or a sequence encoding a retroviridae capsid protein or both. Embodiment 28 The recombinant eukaryotic host cell according to embodiment 27, wherein the cyclic dinucleotide synthase is selected from the group consisting of the diadenylate cyclase, diguanylate cyclase and the cyclic GMP-AMP synthase. Embodiment 29 The recombinant eukaryotic host cell according to embodiment 27 or 28, wherein the cyclic dinucleotide synthase is cGAS (Cyclic GMP-AMP synthase). Embodiment 30 The recombinant eukaryotic host cell according to any one of embodiments 27-29, wherein the recombinant eukaryotic host cell comprises both a sequence encoding a viral fusogenic glycoprotein and a sequence encoding a retroviridae capsid protein. Embodiment 31 The recombinant eukaryotic host cell according to any one of embodiments 27-30, wherein the recombinant eukaryotic host cell further comprises a sequence encoding an antigen or any other protein or nucleic acid of interest. Embodiment 32 The recombinant eukaryotic host cell according to any one of embodiments 27-31, wherein one or several sequences selected from the sequence encoding the cyclic dinucleotide synthase, the viral fusogenic glycoprotein and the sequence encoding a retroviridae capsid protein are episomal. Embodiment 33 The recombinant eukaryotic host cell according to any one of embodiments 27-31, wherein one or several sequences selected from the sequence encoding the cyclic dinucleotide synthase, the viral fusogenic glycoprotein and the sequence encoding retroviridae capsid protein are integrated into the host cell chromosome. Embodiment 34 The recombinant eukaryotic host cell according to any one of embodiments 27-33 as a drug or a vaccine adjuvant. Embodiment 35 A method for inducing or enhancing an immune response in a subject comprising administering a recombinant eukaryotic host cell according to any one of embodiments 27-33. Embodiment 36 A method for preventing or treating an infectious disease or a cancer in a subject comprising administering a recombinant eukaryotic host cell according to any one of embodiments 27-33. Embodiment 37 A method for preparing a virus-like particle comprising cyclic dinucleotides packaged into said virus-like particle, wherein the method comprises: co-expression of a cyclic dinucleotide synthase and a viral fusogenic glycoprotein in a eukaryotic cell in conditions allowing the synthesis of cyclic dinucleotides and the viral fusogenic glycoprotein in said cell; andrecovery of the virus-like particles produced by said cell. Embodiment 38 The method according to embodiment 37, wherein the cyclic dinucleotide synthase is selected from the group consisting of the diadenylate cyclase, diguanylate cyclase and the cyclic GMP-AMP synthase. Embodiment 39 The method according to embodiment 37 or 38, wherein the cyclic dinucleotide synthase is cGAS (Cyclic GMP-AMP synthase). Embodiment 40 The method according to any one of embodiments 37-39, wherein said cell further expresses a capsid from retroviridae. Embodiment 41 The method according to any one of embodiments 37-40, wherein the viral fusogenic glycoprotein is a glycoprotein from retroviridae (including lentivirus and retrovirus), herpesviridae, poxviridae, hepadnaviridae, flaviviridae, togaviridae, coronaviridae, hepatitis D virus, orthomyxoviridae, paramyxoviridae, rhabdoviridae, bunyaviridae, filoviridae, and orthopoxiviridae (e.g., variola), preferably from orthomyxovirus, retroviruses, and rhabdovirus. Embodiment 42 The method according to any one of embodiments 37-41, wherein the viral fusogenic glycoprotein is a glycoprotein from HIV (Human Immunodeficiency Virus) including HIV-1 and HIV-2, Influenza including Influenza A (e.g., subtypes H5N1 and H1N1) and Influenza B, and, thogotovirus, and VSV (Vesicular Stomatitis Virus). Embodiment 43 The method according to any one of embodiments 37-42, wherein the retroviral capsid is from retroviridae, preferably lentivirus and retrovirus, preferably from HIV or MLV (Murine Leukemia Virus).","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"}},"description_lang":["en"],"has_description":true,"has_docdb":true,"has_inpadoc":true,"has_full_text":true,"biblio_lang":"en"},"jurisdiction":"US","collections":[],"usersTags":[],"lensId":"024-804-982-598-966","publicationKey":"US_10010607_B2","displayKey":"US 10010607 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wherein the retroviridae capsid is from HIV or Murine Leukemia Virus (MLV)."],"number":4,"annotation":false,"claim":true,"title":false},{"lines":["The virus-like particle according to claim 1, wherein the viral fusogenic glycoprotein is a glycoprotein from retroviridae, herpesviridae, poxviridae, hepadnaviridae, flaviviridae, togavoridae, coronaviridae, hepatitis D virus, orthomyxoviridae, paramyxoviridae, filoviridae, rhabdoviridae, bunyaviridae, or orthopoxiviridae."],"number":5,"annotation":false,"claim":true,"title":false},{"lines":["The virus-like particle according to claim 1, wherein the viral fusogenic glycoprotein is a glycoprotein from Human Immunodeficiency Virus (HIV), HIV-1, HIV-2, Influenza virus, Influenza virus type A, Influenza virus type B, Thogotovirus, or Vesicular Stomatitis Virus (VSV)."],"number":6,"annotation":false,"claim":true,"title":false},{"lines":["The virus-like particle according to claim 1, wherein the cyclic dinucleotides are 2′-3′-cyclic GMP-AMP."],"number":7,"annotation":false,"claim":true,"title":false},{"lines":["The virus-like particle according to claim 1, wherein the cyclic dinucleotides are 3′-3′-cyclic GMP-AMP."],"number":8,"annotation":false,"claim":true,"title":false},{"lines":["The virus-like particle according to claim 1, further comprising an antigen or a protein or nucleic acid of interest."],"number":9,"annotation":false,"claim":true,"title":false},{"lines":["The virus-like particle according to claim 1 as a drug or a vaccine adjuvant."],"number":10,"annotation":false,"claim":true,"title":false},{"lines":["A pharmaceutical, vaccine or veterinary composition comprising a virus-like particle according to claim 1 and a pharmaceutically acceptable carrier."],"number":11,"annotation":false,"claim":true,"title":false},{"lines":["The pharmaceutical, vaccine or veterinary composition according to claim 11, further comprising an antigen or a therapeutically active agent."],"number":12,"annotation":false,"claim":true,"title":false},{"lines":["A method for inducing or enhancing an immune response in a subject comprising administering a virus-like particle according to claim 1 or a composition according to claim 11."],"number":13,"annotation":false,"claim":true,"title":false},{"lines":["A method for treating an infectious disease or a cancer in a subject comprising administering a virus-like particle according to claim 1 or a composition according to claim 11."],"number":14,"annotation":false,"claim":true,"title":false},{"lines":["A virus-like particle comprising a lipoprotein envelope comprising a viral fusogenic glycoprotein, wherein said virus-like particle contains cGAMP packaged into said virus-like particle wherein the virus-like particle contains at least 0.015 ng/ml of cGAMP."],"number":15,"annotation":false,"claim":true,"title":false},{"lines":["A pharmaceutical, vaccine or veterinary composition comprising a virus-like particle according to claim 15 and a pharmaceutically acceptable carrier."],"number":16,"annotation":false,"claim":true,"title":false},{"lines":["A method for preparing a virus-like particle comprising cyclic dinucleotides packaged into said virus-like particle, wherein the method comprises:\n
co-expression of a cyclic GMP-AMP synthase (cGAS) and a viral fusogenic glycoprotein in a eukaryotic cell in conditions allowing the synthesis of cGAMP and the viral fusogenic glycoprotein in said cell; and\n
recovering the virus-like particles produced by said cell, wherein the virus-like particles comprise cGAMP packaged into said virus-like particle."],"number":17,"annotation":false,"claim":true,"title":false},{"lines":["The method according to claim 17, wherein said cell further expresses a capsid from retroviridae."],"number":18,"annotation":false,"claim":true,"title":false},{"lines":["The method according to claim 17, wherein the viral fusogenic glycoprotein is a glycoprotein from retroviridae, herpesviridae, poxviridae, hepadnaviridae, flaviviridae, togavoridae, coronaviridae, hepatitis D virus, orthomyxoviridae, paramyxoviridae, rhabdoviridae, bunyaviridae, filoviridae, and orthopoxiviridae."],"number":19,"annotation":false,"claim":true,"title":false},{"lines":["The method according to claim 17, wherein the viral fusogenic glycoprotein is a glycoprotein from HIV, HIV-1 and HIV-2, Influenza virus, Influenza virus type A, Influenza virus type B, Thogotovirus, or VSV."],"number":20,"annotation":false,"claim":true,"title":false},{"lines":["The method according to claim 17, wherein the retroviral capsid is from a retroviridae."],"number":21,"annotation":false,"claim":true,"title":false}]}},"filters":{"npl":[],"notNpl":[],"applicant":[],"notApplicant":[],"inventor":[],"notInventor":[],"owner":[],"notOwner":[],"tags":[],"dates":[],"types":[],"notTypes":[],"j":[],"notJ":[],"fj":[],"notFj":[],"classIpcr":[],"notClassIpcr":[],"classNat":[],"notClassNat":[],"classCpc":[],"notClassCpc":[],"so":[],"notSo":[],"sat":[]},"sequenceFilters":{"s":"SEQIDNO","d":"ASCENDING","p":0,"n":10,"sp":[],"si":[],"len":[],"t":[],"loc":[]}}