Influenza virus vaccine composition and methods of use
| Title: | Influenza virus vaccine composition and methods of use |
|---|---|
| Patent Number: | 7,785,603 |
| Publication Date: | August 31, 2010 |
| Appl. No: | 11/715973 |
| Application Filed: | March 09, 2007 |
| Abstract: | The present invention is directed to enhancing the immune response of a human in need of protection against IV infection by administering in vivo, into a tissue of the human, at least one polynucleotide comprising one or more regions of nucleic acid encoding an IV protein or a fragment, a variant, or a derivative thereof. The present invention is further directed to enhancing the immune response of a human in need of protection against IV infection by administering, in vivo, into a tissue of the human, at least one IV protein or a fragment, a variant, or derivative thereof. The IV protein can be, for example, in purified form or can be an inactivated IV, such as those present in inactivated IV vaccines. The polynucleotide is incorporated into the cells of the human in vivo, and an immunologically effective amount of an immunogenic epitope of an IV, or a fragment, variant, or derivative thereof is produced in vivo. The IV protein (in purified form or in the form of an inactivated IV vaccine) is also administered in an immunologically effective amount. |
| Inventors: | Luke, Catherine J. (Frederick, MD, US); Vilalta, Adrian (San Diego, CA, US); Wloch, Mary K. (San Diego, CA, US); Evans, Thomas G. (Cambridge, MA, US); Geall, Andrew J. (Littleton, MA, US); Jimenez, Gretchen S. (San Diego, CA, US) |
| Assignees: | Vical Incorporated (San Diego, CA, US) |
| Claim: | 1. An isolated polynucleotide comprising a first nucleic acid fragment, which encodes the amino acid sequence of SEQ ID NO:78 and a second nucleic acid fragment which encodes the amino acid sequence of SEQ ID NO:76, wherein the codons of said first and second nucleic acid fragments are optimized for expression in humans. |
| Claim: | 2. The polynucleotide of claim 1 , wherein the nucleotide sequence of said first nucleic acid fragment is SEQ ID NO:66 and wherein the nucleotide sequence of said second nucleic acid fragment is SEQ ID NO:75. |
| Claim: | 3. A vector comprising the polynucleotide of claim 1 , wherein said vector, upon uptake by a suitable host cell, expresses said amino acid sequences of SEQ ID NO:78 and SEQ ID NO:76. |
| Claim: | 4. The vector of claim 3 , wherein said amino acid sequences of SEQ ID NO:78 and SEQ ID NO:76 are expressed as a fusion protein. |
| Claim: | 5. A vector comprising the polynucleotide of claim 1 , wherein said vector is DNA and wherein said vector comprises a first expression cassette and second expression cassette, said first expression cassette comprises a first nucleic acid fragment, which encodes the amino acid sequence of SEQ ID NO:78 in operable association with a promoter, and said second expression cassette comprises a second nucleic acid fragment which encodes the amino acid sequence of SEQ ID NO:76 in operable association with a promoter. |
| Claim: | 6. The vector of claim 5 , wherein said first expression cassette and said second expression cassette are associated with separate promoters. |
| Claim: | 7. The vector of claim 6 , wherein said separate promoters are non-identical. |
| Claim: | 8. The vector of claim 5 , wherein said first expression cassette and said second expression cassette are associated with a single promoter, and wherein said second expression cassette is in operable association with an internal ribosome entry site (IRES). |
| Claim: | 9. The vector of claim 5 , wherein said first expression cassette and said second expression cassette are associated with a single promoter, and wherein said first expression cassette is in operable association with an internal ribosome entry site (IRES). |
| Claim: | 10. A composition comprising the vector of claim 3 and a carrier. |
| Claim: | 11. A composition comprising the vector of claim 5 and a carrier. |
| Claim: | 12. A composition comprising at least two non-identical vectors, wherein one of said vectors comprises a nucleic acid fragment which encodes the amino acid sequence of SEQ ID NO:78 and wherein another of said vectors comprises a nucleic acid fragment which encodes the amino acid sequence of SEQ ID NO:76, wherein the codons of said nucleic acid fragments encoding SEQ ID NO:78 and SEQ ID NO:76 are optimized for expression in humans, and wherein said vectors, upon uptake by a suitable host cell, express said amino acid sequences. |
| Claim: | 13. The composition of claim 12 , further comprising a carrier. |
| Claim: | 14. The composition of claim 13 , further comprising a component selected from the group consisting of an adjuvant and a transfection facilitating compound. |
| Claim: | 15. The composition of claim 14 , wherein said component is a cationic lipid. |
| Claim: | 16. The composition of claim 14 , wherein said adjuvant comprises (±)-N-(3-aminopropyl)-N,N-dimethyl-2,3-bis(syn-9-tetradeceneyloxy)-1-propanaminium bromide (GAP-DMORIE) and a neutral lipid, wherein said neutral lipid is selected from the group consisting of: (a) 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE); (b) 1,2-diphytanoyl-sn-glycero-3-phosphoethanolamine (DPyPE); and (d) 1,2-dimyristoyl-glyccro-3-phosphoethanolamine (DMPE). |
| Claim: | 17. The composition of claim 15 , wherein said transfection facilitating compound comprises ()N-(2-hydroxyethyl)-N,N-dimethyl-2,3-bis(tetradecyloxy)-1-propanaminium bromide (DMRTE). |
| Claim: | 18. The composition of claim 17 , wherein said transfection facilitating compound further comprises a neutral lipid. |
| Claim: | 19. The composition of claim 18 , wherein the neutral lipid is DOPE. |
| Claim: | 20. The composition of claim 16 further comprising a 1:1 molar ratio of GAP-DMORIE and DPyPE. |
| Claim: | 21. A method for treating or preventing influenza infection in a vertebrate comprising administering to a vertebrate in need thereof the composition of claim 13 . |
| Claim: | 22. A method for eliciting an immune response to influenza virus in a vertebrate by administration of the composition of claim 13 . |
| Claim: | 23. A method for treating or preventing influenza infection in a vertebrate comprising administering to a vertebrate in need thereof the composition of claim 10 . |
| Claim: | 24. A method for eliciting an immune response to influenza virus in a vertebrate by administration of the composition of claim 10 . |
| Claim: | 25. A method for treating or preventing influenza infection in a vertebrate comprising administering to a vertebrate in need thereof the composition of claim 11 . |
| Claim: | 26. A method for eliciting an immune response to influenza virus in a vertebrate by administration of the composition of claim 11 . |
| Current U.S. Class: | 4242/091 |
| Patent References Cited: | 4683195 July 1987 Mullis et al. 4816567 March 1989 Cabilly et al. 4818527 April 1989 Thornton et al. 4882145 November 1989 Thornton et al. 5143726 September 1992 Thornton et al. 5264618 November 1993 Felgner et al. 5561064 October 1996 Marquet et al. 5580859 December 1996 Felgner et al. 5591631 January 1997 Leppla et al. 5656611 August 1997 Kabanov et al. 5837693 November 1998 German et al. 6004944 December 1999 Rothman et al. 6207646 March 2001 Krieg et al. 6214804 April 2001 Felgner et al. 6231864 May 2001 Birkett 6406705 June 2002 Davis et al. 6429199 August 2002 Krieg et al. 6500432 December 2002 Dalemans et al. 6867195 March 2005 Felgner et al. 6875748 April 2005 Manthorpe et al. 7105574 September 2006 Wheeler 7250404 July 2007 Felgner et al. 2002/0165172 November 2002 Sallberg et al. 2003/0032615 February 2003 Felgner et al. 2003/0191082 October 2003 Wheeler 2004/0023911 February 2004 Felgner et al. 2004/0157244 August 2004 Budahazi et al. 2004/0157789 August 2004 Geall 2004/0162256 August 2004 Geall et al. 2004/0171572 September 2004 Wheeler 2006/0024670 February 2006 Luke et al. 2007/0286869 December 2007 Luke et al. 2 025 598 March 1991 0 173 494 March 1986 0 171 496 May 1993 0 385 610 March 1994 0 421 635 July 1995 WO 86/01533 March 1986 WO 87/02671 May 1987 WO 94/21797 September 1994 WO 99/40934 August 1999 WO 00/57917 October 2000 WO 01/83528 November 2001 WO 02/00844 January 2002 WO 02/24876 March 2002 |
| Other References: | Bender, B.S., et al., “Immunogenicity and efficacy of DNA vaccines encoding influenza A proteins in aged mice,” Vaccine 16:1748-1755, Elsevier Science Ltd. (1998). cited by other Bryder, K., et al., “Improved Immunogenicity of HIV-1 Epitopes in HbsAg Chimeric DNA Vaccine Plasmids by Structural Mutations of HbsAg,” DNA Cell Biol. 18:219-225, Mary Ann Liebert, Inc. (1999). cited by other Deml, L., et al., “Multiple Effects of Codon Usage Optimization on Expression and Immunogenicity of DNA Candidate Vaccines Encoding the Human Immunodeficiency Virus Type 1 Gag Protein,” J. Virol. 75:10991-11001, American Society for Microbiology (2001). cited by other Gaschen, B., et al., “Diversity Considerations in HIV-1 Vaccine Selection,” Science 296:2354-2360, American Association for the Advancement of Science (2002). cited by other Liu, W.J., et al., “Polynucleotide viral vaccines: codon optimisation and ubiquitin conjugation enhances prophylactic and therapeutic efficacy,” Vaccine 20:862-869, Elsevier Science Ltd. (2002). cited by other International Search Report for International Application No. PCT/US05/17157, mailed on Oct. 25, 2007, ISA/US, Alexandria, VA. cited by other U.S. Appl. No. 11/892,016, inventors Luke et al., filed Aug. 17, 2007. cited by other Aihara, H. and Miyazaki J.-I., “Gene transfer into muscle by electroporation in vivo,” Nat. Biotechnol. 16:867-870, Nature America, Inc. (1998). cited by other Attal, J., et al., “The RU5 (‘R’) region from human leukaemia viruses (HTLV-1) contains an internal ribosome entry site (IRES)-like sequence,” FEBS Letters 392:220-224, Elsevier Science B.V. (1996). cited by other Berendt, R.F. and Hall, W.C., “Reaction of Squirrel Monkeys to Intratracheal Inoculation with Influenza/A/New Jersey/76 (Swine) Virus,” Infect. Immun. 16:476-479, American Society for Microbiology (1977). cited by other Billaut-Mulot, O., et al., “Interleukin-18 modulates immune responses induced by HIV-1 Nef DNA prime/protein boost vaccine,” Vaccine 19:95-102, Elsevier Science Ltd. (2001). cited by other Boulianne, G.L., et al., “Production of functional chimaeric mouse/human antibody,” Nature 312:643-646, Macmillan Journals Ltd. (1984). cited by other Chen, Z.-Y., et al., “Linear DNAs Concatemerize in Vivo and Result in Sustained Transgene Expression in Mouse Liver,” Mol. Ther. 3:403-410, Academic Press (2001). cited by other Cherng, J.-Y., et al., “Effect of DNA topology on the transfection efficiency of poly((2-dimethylamino)ethyl methacrylate)-plasmid complexes,” J. Control. Release 60:343-353, Elsevier Science B.V. (1999). cited by other Clarke, B.E., et al., “Improved immunogenicity of a peptide epitope after fusion to hepatitis B core protein,” Nature 330:381-384, Macmillan Magazines Ltd. (1987). cited by other Collins, P.L., et al., “Respiratory Syncytial Virus,” in Field's Virology, 4th Edition, Knipe, D.M., et al., eds., Lipponcott Williams & Wilkins, Chapter 45, pp. 1464-1465 (2001). cited by other Colucci, G., et al., “Identification of a Major Hepatitis B Core Antigen (HBcAg) Determinant by Using Synthetic Peptides and Monoclonal Antibodies,” J. Immunol. 141:4376-4380, The American Association of Immunologists (1988). cited by other Crasto, C.J. and Feng, J.-A., “Linker: a program to generate linker sequences for fusion proteins,” Protein Eng. 13:309-312, Oxford University Press (2000). cited by other Darquet, A.-M., et al.,“A new DNA vehicle for nonviral gene delivery: supercoiled minicircle,” Gene Therapy 4:1341-1349, Stockton Press (1997). cited by other Davis, H.L., et al., “Direct gene transfer in skeletal muscle: plasmid DNA-based immunization against the hepatitis B virus surface antigen,” Vaccine 12:1503-1509, Butterworth-Heinemann Ltd. (1994). cited by other Donnelly, J.J., et al., “DNA Vaccines,” Annu. Rev. Immunol. 15:617-648, Annual Reviews Inc. (1997). cited by other Felgner, P.L., et al., “Lipofection: A highly efficient, lipid-mediated DNA-transfection procedure,” Proc. Natl. Acad. Sci. USA 84:7413-7417, The National Academy of Sciences (1987). cited by other Fischer, W.B. And Sansom, M.S., “Viral ion channels: structure and function,” Biochim. Biophys. Acta 1561:27-45, Elsevier Science B.V. (2002). cited by other Galibert, F., et al., “Nucleotide sequence of the hepatitis B virus genome (subtype ayw) cloned in E. coli,” Nature 281:646-650, Macmillan Journals Ltd. (1979). cited by other Gao, X. and Huang, L., “Potentiation of Cationic Liposome-Mediated Gene Delivery by Polycations,” Biochemistry 35:1027-1036, American Chemical Society (1996). cited by other Gilbert, S.C., et al., “Enhanced CD8 T cell immunogenicity and protective efficacy in a mouse malaria model using a recombinant adenoviral vaccine in heterologous prime-boost immunisation regimes,” Vaccine 20:1039-1045, Elsevier Science Ltd. (2002). cited by other Goff, S.P., “Retroviridae: The Retroviruses and Their Replication,” in Field's Virology, 4th Edition, Knipe, D.M., et al., eds., Lipponcott Williams & Wilkins, Chapter 57, pp. 1871-1939 (2001). cited by other Gonzalo, R.M., et al., “A heterologous prime-boost regime using DNA and recombinant vaccinia virus expressing the Leishmania infantum P36/LACK antigen protects BALB/c mice from cutaneous leishmaniasis,” Vaccine 20:1226-1231, Elsevier Science Ltd. (2002). cited by other Graham, F.L. and Van Der Eb, A.J., “A New Technique for the Assay of Infectivity of Human Adenovirus 5 DNA,” Virology 52:456-467, Academic Press, Inc. (1973). cited by other Gramzinski, R.A., et al., “Immune Response to a Hepatitis B DNA Vaccine in Aotus Monkeys: A Comparison of Vaccine Formulation, Route, and Method of Administration,” Mol. Med. 4:109-118, The Picower Institute Press (1998). cited by other National Research Council, Guide for the Care and Use of Laboratory Animals, National Academy Press, Washington, D.C. (1996). cited by other Macken, C., et al., “The value of a database in surveillance and vaccine selection,” in Options for the Control of Influenza IV, Osterhaus, A.D.M.E., et al., eds., Elsevier Science B.V., Amsterdam, pp. 103-106 (2001). cited by other Hartikka, J., et al., “Vaxfectin enhances the humoral immune response to plasmid DNA-encoded antigens,” Vaccine 19:1911-1923, Elsevier Science Ltd. (2001). cited by other Hartikka, J., et al., “Electroporation-Facilitated Delivery of Plasmid DNA in Skeletal Muscle: Plasmid Dependence of Muscle Damage and Effect of Poloxamer 188,” Mol Ther 4:407-415, Academic Press (2001). cited by other Hartikka, J., et al., “An Improved Plasmid DNA Expression Vector for Direct Injection into Skeletal Muscle,” Hum. Gene Ther. 7:1205-1217, Mary Ann Liebert, Inc. (1996). cited by other Heinen, P.P., et al., “Vaccination of pigs with a DNA construct expressing an influenza virus M2-nucleoprotein fusion protein exacerbates disease after challenge with influenza A virus,” J. Gen. Virol. 83:1851-1859, Society for General Microbiology (2002). cited by other Horn, N.A., et al., “Cancer Gene Therapy Using Plasmid DNA: Purification of DNA for Human Clinical Trials,” Hum. Gene Ther. 6:565-573, Mary Ann Liebert, Inc. (1995). cited by other Ito, T., et al., “Evolutionary Analysis of the Influenza A Virus M Gene with Comparison of the M1 and M2 Proteins,” J. Virol. 65:5491-5498, American Society for Microbiology (1991). cited by other Jung, J., et al., “Distinct Response of Human B cell Subpopulations in Recognition of an Innate Immune Signal, CpG DNA,” J. Immunol. 169:2368-2373, The American Association of Immunologists, Inc. (2002). cited by other Klinman, D.M., et al., “CpG motifs present in bacterial DNA rapidly induce lymphocytes to secrete interleukin 6, interleukin 12, and interferon γ,” Proc. Natl Acad. Sci. USA 93:2879-2883, The National Academy of Sciences (1996). cited by other Kodihalli, S., et al., “Strategies for inducing protection against avian influenza A virus subtypes with DNA vaccines,” Vaccine 18:2592-2599, Elsevier Science Ltd. (2000). cited by other Köhler, G., et al., “Fusion between immunoglobulin-secreting and nonsecreting myeloma cell lines,” Eur. J. Immunol. 6:292-295, Verlag Chemie, GmbH and Academic Press Inc. (1976). cited by other Köhler, G. and Milstein, C., “Derivation of specific antibody-producing tissue culture and tumor lines by cell fusion,” Eur. J. Immunol. 6:511-519, Verlag Chemie, GmbH and Academic Press Inc. (1976). cited by other Köhler, G. and Milstein, C., “Continuous cultures of fused cells secreting antibody of predefined specificity,” Nature 256:495-497, Macmillan Journals Ltd. (1975). cited by other Lamb, R.A. and Lai, C.-J., “Conservation of the Influenza Virus Membrane Protein (M1) Amino Acid Sequence and an Open Reading Frame of RNA Segment 7 Encoding a Second Protein (M2) in H1N1 and H3N2 Strains,” Virology 112:746-751, Academic Press, Inc. (1981). cited by other Lamb, R.A., et al., “Influenza Virus M2 Protein Is an Integral Membrane Protein Expressed on the Infected-Cell Surface,” Cell 40:627-633, The MIT Press (1985). cited by other Lindmayer, I., et al., “Development of New Jet Injector for Insulin Therapy,” Diabetes Care 9:294-297, American Diabetes Association, Inc. (1986). cited by other Manickan, E., et al., “DNA Vaccines—A Modern Gimmick or a Boon to Vaccinology?” Crit. Rev. Immunol. 17:139-154, Begell House, Inc. (1997). cited by other Martins, J.K. and Roedl, E.A., “Medijector—A New Method of Corticosteroid-Anesthetic Delivery,” J. Occup. Med. 21:821-824, Oxford University Press (1979). cited by other Mathiesen, I., “Electropermeabilization of skeletal muscle enhances gene transfer in vivo,” Gene Ther. 6:508-514, Stockton Press (1999). cited by other Mir, L.M., et al., “High-efficiency gene transfer into skeletal muscle mediated by electric pulses,” Proc. Natl Acad. Sci. USA 96:4262-4267, The National Academy of Sciences (1999). cited by other Morrison, S.L., “Transfectomas Provide Novel Chimeric Antibodies,” Science 229:1202-1207, American Association for the Advancement of Science (1985). cited by other Nakamura, Y., et al., “Codon usage tabulated from international DNA sequence databases: status for the year 2000,” Nucl. Acids Res. 28:292, Oxford University Press (2000). cited by other Nassal, M., “Total chemical synthesis of a gene for hepatitis B virus core protein and its functional characterization,” Gene 66:279-294, Elsevier Science Publishers B.V. (1988). cited by other Neirynck, S., et al., “A universal influenza A vaccine based on the extracellular domain of the M2 protein,” Nat. Med. 5:1157-1163, Nature America, Inc. (1999). cited by other Neuberger, M.S., et al., “A hapten-specific chimaeric IgE antibody with human physiological effector function,” Nature 314:268-270, Macmillan Journals Ltd. (1985). cited by other Nossal, G., “Living up to the legacy,” Nat. Med. 4(Vaccine Suppl.):475-476, Nature America, Inc. (1998). cited by other Oi, V.T. and Morrison, S.L., “Chimeric Antibodies,” BioTechniques 4:214-221, Eaton Publishing Co. (1986). cited by other Okuda, K., et al., “Protective immunity against influenza A virus induced by immunization with DNA plasmid containing influenza M gene,” Vaccine 19:3681-3691, Elsevier Science Ltd. (2001). cited by other Qin, Y.-J., et al., “Gene Suture—A Novel Method for Intramuscular Gene Transfer and Its Application in Hypertension Therapy,” Life Sciences 65: 2193-2203, Elsevier Science Inc. (1999). cited by other Rizzuto, G., et al., “Gene Electrotransfer Results in a High-Level Transduction of Rat Skeletal Muscle and Corrects Anemia of Renal Failure,” Hum. Gen. Ther. 11:1891-1900, Mary Ann Liebert, Inc. (2000). cited by other Robinson, H.L., “New Hope for an AIDS Vaccine,” Nat. Rev. Immunol. 2:239-250, Nature Publishing Group (2002). cited by other Salfeld, J., et al. “Antigenic Determinants and Functional Domains in Core Antigen and e Antigen from Hepatitis B Virus,” J. Virol. 63:798-808, American Society for Microbiology (1989). cited by other Sankar, V., et al., “Salivary gland delivery of pDNA-cationic lipoplexes elicits systemic immune responses,” Oral Diseases 8:275-281, Blackwell Munksgaard (2002). cited by other Schneider, J., et al., “Induction of CD8+ T cells using heterologous prime-boost immunisation strategies,” Immunol. Rev. 170:29-38, Munksgaard Inetrnational Publishers Ltd. (1999). cited by other Schrijver, R.S., et al., “Immunization of cattle with a BHV1 vector vaccine or a DNA vaccine both coding for the G protein of BRSV,” Vaccine 15:1908-1916, Elsevier Science Ltd. (1997). cited by other Shiver, J.W., et al., “Replication-incompetent adenoviral vaccine vector elicits effective anti-immunodeficiency-virus immunity,” Nature 415:331-335, Nature Publishing Group (2002). cited by other Shu, L.L., et al., “Analysis of the Evolution and Variation of the Human Influenza A Virus Nucleoprotein Gene from 1933 to 1990,” J. Virol. 67:2723-2729, American Society for Microbiology (1993). cited by other Sin, J.-I., et al., “DNA Priming-Protein Boosting Enhances Both Antigen-Specific Antibody and Th1-Type Cellular Immune Responses in a Murine Herpes Simplex Virus-2 gD Vaccine Model,” DNA Cell Biol. 18:771-779, Mary Ann Liebert, Inc. (1999). cited by other Slepushkin, V.A., et al., “Protection of mice against influenza A virus challenge by vaccination with baculovirus-expressed M2 protein,” Vaccine 13:1399-1402, Elsevier Science Ltd. (1995). cited by other Stahl, S.J. and Murray, K., “Immunogenicity of peptide fusions to hepatitis B virus core antigen,” Proc. Natl. Acad. Sci. USA, 86:6283-6287, The National Academy of Sciences (1989). cited by other Subbarao, K., “Influenza Vaccines: Present and Future,” Advances in Virus Research 54:349-373, Academic Press (1999). cited by other Sutcliffe, J.G., et al., “Antibodies That React with Predetermined Sites on Proteins,” Science 219:660-666, American Association for the Advancement of Science (1983). cited by other Takebe, Y., et al., “SRα Promoter: an Efficient and Versatile Mammalian cDNA Expression System Composed of the Simian Virus 40 Early Promoter and the R-U5 Segment of Human T-Cell Leukemia Virus Type 1 Long Terminal Repeat,” Mol. Cell Biol. 8:466-472, American Society for Microbiology (1988). cited by other Tanghe, A., “Improved Immunogenicity and Protective Efficacy of a Tuberculosis DNA Vaccine Encoding Ag85 by Protein Boosting,” Infect. Immun. 69:3041-3047, American Society for Microbiology (2001). cited by other Toncheva, V., et al., “Novel vectors for gene delivery formed by self-assembly of DNA with poly(L-lysine) grafted with hydrophilic polymers,” Biochim. Biophys. Acta 1380:354-368, Elsevier Science B.V. (1998). cited by other Treanor, J.J., et al., “Passively Transferred Monoclonal Antibody to the M2 Protein Inhibits Influenza A Virus Replication in Mice,” J. Virol. 64:1375-1377, American Society for Microbiology (1990). cited by other Trubetskoy, V.S., et al., “Cationic liposomes enhance targeted delivery and expression of exogenous DNA mediated by N-terminal modified poly(L-lysine)-antibody conjugate in mouse lung endothelial cells,” Biochem. Biophys. Acta 1131:311-313, Elsevier Science Publishers B.V. (1992). cited by other Ulmer, J.B., et al., “Protective CD4+ and CD8+T cells against Influenza Virus Induced by Vaccination with Nucleoprotein DNA,” J Virol. 72:5648-5653, American Society for Microbiology (1998). cited by other Ulmer, J.B., et al., “Heterologous Protection Against Influenza by Injection of DNA Encoding a Viral Protein,” Science 259:1745-1749, American Association for the Advancement of Science (1993). cited by other Vahlsing, H.L., et al., “Immunization with plasmid DNA using a pneumatic gun,” J. Immunol. Methods 175:11-22, Elsevier Science B.V. (1994). cited by other Wagner, H., “Interactions between bacterial CpG-DNA and TLR9 bridge innate and adaptive immunity,” Curr. Opin. Microbiol. 5:62-69, Elsevier Science Ltd. (2002). cited by other Wands, J.R. and Zurawski, Jr., V.R., “High Affinity Monoclonal Antibodies to Hepatitis B Surface Antigen (HBsAg) Produced by Somatic Cell Hybrids,” Gastroenterology 80:225-232, Elsevier North-Holland, Inc. (1981). cited by other Watabe, S., et al., “Protection against influenza virus challenge by topical application of influenza DNA vaccine,” Vaccine 19:4434-4444, Elsevier Science Ltd. (2001). cited by other Wheeler, C.J., et al., “Converting an alcohol to an amine in a cationic lipid dramatically alters the co-lipid requirement, cellular transfection activity and the ultrastructure of DNA-cytofectin complexes,” Biochim. Biophys. Acta 1280:1-11, Elsevier Science B.V. (1996). cited by other Wheeler, C.J., et al., “A novel cationic lipid greatly enhances plasmid DNA delivery and expression in mouse lung,” Proc. Natl. Acad. Sci. USA 93:11454-11459, The National Academy of Sciences (1996). cited by other Widera, G., et al, “Increased DNA Vaccine Delivery and Immunogenicity by Electroporation In Vivo,” J. Immunol. 164:4635-4640, The American Association of Immunologists (2000). cited by other Yang, Z.-Y., et al. “Overcoming Immunity to a Viral Vaccine by DNA Priming before Vector Boosting,” J. Virol. 77:799-803, American Society for Microbiology (2003). cited by other Yanisch-Perron, C., et al. “Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors,” Gene 33:103-119, Elsevier Science Publishers (1985). cited by other Zhong, Q., et al., “The M2 channel of influenza A virus: a molecular dynamics study,” FEBS Lett. 434:265-271, Elsevier Science B.V. (1998). cited by other NCBI Entrez, GenBank Report, Accession No. K01395 (Entry date 1993). cited by other NCBI Entrez, GenBank Report, Accession No. AF046098 (Entry date 1998). cited by other NCBI Entrez, GenBank Report, Accession No. AF116576 (Entry date 1999). cited by other NCBI Entrez, GenBank Report, Accession No. AF202541 (Entry date 1999). cited by other NCBI Entrez, GenBank Report, Accession No. AF389121 (Entry date 2001). cited by other NCBI Entrez, GenBank Report, Accession No. AJ404626 (Entry date 2000). cited by other NCBI Entrez, GenBank Report, Accession No. M38279 (Entry date 1993). cited by other Co-pending U.S. Appl. No. 60/681,975, inventors Hermanson, G., et al., filed May 18, 2005. cited by other “Codon Usage Database” maintained by Kazusa DNA Research Institute, 1 page, available at http://www.kazusa.or.jp/codon/ (visited Jul. 9, 2002). cited by other Mozdzanowska, K., et al., “Induction of influenza type A virus-specific resistance by immunization of mice with a synthetic multiple antigenic peptide vaccine that contains ectodomains of matrix protein 2,” Vaccine 21:2616-2626, Elsevier Science (Jun. 2003). cited by other Koide, Y., et al., “DNA vaccines,” Jpn. J. Pharmacol. 83:167-174, Japanese Pharmacological Society (Jul. 2000). cited by other NCBI Entrez, GenBank Report, Accession No. CAD30535, Gregory, V., et al. (first entered 2002, last updated Nov. 2006). cited by other NCBI Entrez, GenBank Report, Accession No. AAA19192, Klimov,A.I., et al., (first entered 1992, last updated Jun. 2006). cited by other Lindstrom, S.E., et al., “Phylogenetic Analysis of the Entire Genome of Influenza A (H3N2) Viruses from Japan: Evidence for Genetic Reassortment of the Six Internal Genes,” J. Virol. 72:8021-8031, American Society for Microbiology (1998). cited by other NCBI Database, GenBank Report, Accession No. AAC63479, “M1 protein [Influenza A virus H3N2],” 2 pages (first available 1998). cited by other NCBI Database, GenBank Report, Accession No. AAC63480, “M2 protein [Influenza A virus H3N2],” 2 pages (first available 1998). cited by other NCBI Database, GenBank Report, Accession No. AF038271, “Influenza A virus H3N2 A/Niigata/137/96 matrix protein M1 and transmembrane ion channel M2 protein (M) gene, complete cds,” 2 pages (first available 1998). cited by other NCBI Database, GenBank Report, Accession No. Q38SQ6, “Matrix protein 1 (M1),” 3 pages (first available Jan. 2007). cited by other NCBI Database, GenBank Report, Accession No. Q76V11, “Matrix protein 2 (Protein channel protein M2),” 3 pages (first available 1991). cited by other |
| Primary Examiner: | Mosher, Mary E |
| Attorney, Agent or Firm: | Sughrue Mion, PLLC |
| Accession Number: | edspgr.07785603 |
| Database: | USPTO Patent Grants |
| Language: | English |
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