Naturally occurring antibodies in humans can neutralize a variety of influenza virus strains, including H3, H1, H2, and H5

Journal of Virology

Volumn 85, Issue 21, 2011, Pages 11048-11057

  Ohshima, Nobuko ^a   Iba, Yoshitaka ^a   Kubota Koketsu, Ritsuko ^b   Asano, Yoshizo ^c,e   Okuno, Yoshinobu ^d   Kurosawa, Yoshikazu ^a  

^a FUJITA HEALTH UNIVERSITY   (Japan)

^b OSAKA UNIVERSITY   (Japan)

^c FUJITA HEALTH UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^d The Research Foundation for Microbial Diseases of Osaka University   (Japan)

^e HOKKAIDO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

C179 ANTIBODY; EPITOPE; F026 427 ANIBODY; F045 092 ANIBODY; INFLUENZA VIRUS HEMAGGLUTININ; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; SERINE; UNCLASSIFIED DRUG; VIRUS ANTIBODY;

ANTIBODY COMBINING SITE; ANTIBODY LIBRARY; ANTIBODY SPECIFICITY; ANTIGEN BINDING; APHERESIS; ARTICLE; B LYMPHOCYTE; CONTROLLED STUDY; FLOW CYTOMETRY; GENE; HEMAGGLUTINATION INHIBITION; HUMAN; HUMAN CELL; INFLUENZA VIRUS A H1N1; INFLUENZA VIRUS A H2N2; INFLUENZA VIRUS A H3N2; INFLUENZA VIRUS A H5N1; MEDICAL TECHNOLOGY; MOLECULAR CLONING; NONHUMAN; PHAGE DISPLAY; PRIORITY JOURNAL; PROTEIN BINDING; VH1 69 GENE; VIRUS HEMAGGLUTINATION; VIRUS ISOLATION; VIRUS NEUTRALIZATION; VIRUS STRAIN;

ANTIBODIES, NEUTRALIZING; ANTIBODIES, VIRAL; B-LYMPHOCYTES; CROSS REACTIONS; EPITOPES; HEMAGGLUTINATION INHIBITION TESTS; HEMAGGLUTININ GLYCOPROTEINS, INFLUENZA VIRUS; HUMANS; INFLUENZA A VIRUS; MOLECULAR SEQUENCE DATA; NEUTRALIZATION TESTS; PEPTIDE LIBRARY; PROTEIN BINDING; SEQUENCE ANALYSIS, DNA;

INFLUENZA A VIRUS; ORTHOMYXOVIRIDAE;

EID: 80055111172     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.05397-11     Document Type: Article

References (31)

1. Bebbington, C. R., et al. 1992. High-level expression of a recombinant antibody from myeloma cells using a glutamine synthetase gene as an amplifiable selectable marker. Biotechnology (NY) 10:169-175.
2. Bullough, P. A., F. M. Hughson, J. J. Skehel, and D. C. Wiley. 1994. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371:37-43.
3. Chan, C. H., K. G. Hadlock, S. K. H. Foung, and S. Levy. 2001. VH1-69 gene is preferentially used by hepatitis C virus-associated B cell lymphomas and by normal B cells responding to the E2 viral antigen. Blood 97:1023-1026.
4. Ekiert, D. C., et al. 2009. Antibody recognition of a highly conserved influenza virus epitope. Science 324:246-251.
5. Gerhard, W., K. Mozdzanowska, M. Furchner, G. Washko, and K. Maiese. 1997. Role of the B-cell response in recovery of mice from primary influenza virus infection. Immunol. Rev. 159:95-103.
6. Huang, C.-C., et al. 2004. Structural basis of tyrosine sulfation and VH-gene usage in antibodies that recognize the HIV type 1 coreceptor-binding site on gp120. Proc. Natl. Acad. Sci. U. S. A. 101:2706-2711.
7. Iba, Y., K. Ito, and Y. Kurosawa. 1997. Expression vectors for the introduction of highly diverged sequences into the six complementarity-determining regions of an antibody. Gene 194:35-46.
8. Ichihara, Y., H. Matsuoka, and Y. Kurosawa. 1988. Organization of human immunoglobulin heavy chain diversity gene loci. EMBO J. 7:4141-4150.
9. Isoda, N., et al. 2006. Pathogenicity of a highly pathogenic avian influenza virus, A/chicken/Yamaguchi/7/04(H5N1) in different species of birds and mammals. Arch. Virol. 151:1267-1279.
10. Ito, W., and Y. Kurosawa. 1993. Development of an artificial antibody system with multiple valency using an Fv fragment fused to a fragment of protein A. J. Biol. Chem. 268:20668-20675.
11. Kashyap, A. K., et al. 2008. Combinatorial antibody libraries from survivors of the Turkish H5N1 avian influenza outbreak reveal virus neutralization strategies. Proc. Natl. Acad. Sci. U. S. A. 105:5986-5991.
12. Marks, J. D., et al. 1991. By-passing immunization. Human antibodies from V-gene libraries displayed on phage. J. Mol. Biol. 222:581-597.
13. Morino, K., et al. 2001. Antibody fusions with fluorescent proteins: a versatile regent for profiling protein expression. J. Immunol. Methods 257:175-184.
14. Nakagawa, N., R. Kubota, T. Nakagawa, and Y. Okuno. 2001. Antigenic variants with amino acid deletions clarify a neutralizing epitope specific for influenza B virus Victoria group strains. J. Gen. Virol. 82:2169-2172.
15. Nakajima, K., E. Nobusawa, A. Nagy, and S. Nakajima. 2005. Accumulation of amino acid substitutions promotes irreversible structural changes in the hemagglutinin of human influenza AH3 virus during evolution. J. Virol. 79:4672-4677.
16. Okada, J., et al. 2010. Monoclonal antibodies in man that neutralized H3N2 influenza viruses were classified into three groups with distinct strain specificity: 1968-1973, 1977-1993 and 1997-2003. Virology 397:322-330.
17. Okada, J., et al. 2011. Localization of epitopes recognized by monoclonal antibodies that neutralized the H3N2 influenza viruses in man. J. Gen. Virol. 92:326-335.
18. Okuno, Y., et al. 1990. Rapid focus reduction neutralization test of influenza A and B viruses in microtiter system. J. Clin. Microbiol. 28:1308-1313.
19. Okuno, Y., Y. Isegawa, F. Sasao, and S. Ueda. 1993. A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains. J. Virol. 67:2552-2558.
20. Palese, P. 2004. Influenza: old and new threats. Nat. Med. 10:S82-S87.
21. Shirai, H., A. Kidera, and H. Nakamura. 1999. H3-rules: identification of CDR-H3 structures in antibodies. FEBS Lett. 455:188-197.
22. Simmons, C. P., et al. 2007. Prophylactic and therapeutic efficacy of human monoclonal antibodies against H5N1 influenza. PLoS Med. 4:e178.
23. Skehel, J. J., and D. C. Wiley. 2000. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 69:531-569.
24. Sui, J., et al. 2009. Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses. Nat. Struct. Mol. Biol. 16:265-273.
25. Throsby, M., et al. 2008. Heterosubtypic neutralizing monoclonal antibodies cross-protective against H5N1 and H1N1 recovered from human IgM_memory B cells. PLoS One 3:e3942.
26. Ueda, M., et al. 1998. Application of subtype-specific monoclonal antibodies for rapid detection and identification of influenza A and B viruses. J. Clin. Microbiol. 36:340-344.
27. Underwood, P. A. 1982. Mapping of antigenic changes in the haemagglutinin of Hong Kong influenza (H3N2) strains using a large panel of monoclonal antibodies. J. Gen. Virol. 62:153-169.
28. Weis, W., et al. 1988. Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature 333:426-431.
29. Wiley, D. C., I. A. Wilson, and J. J. Skehel. 1981. Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation. Nature 289:373-378.
30. Wrammert, J., et al. 2011. Broadly cross-reactive antibodies dominate the human B cell response against 2009 pandemic H1N1 influenza virus infection. J. Exp. Med. 208:181-193.
31. Yoshida, R., et al. 2009. Cross-protective potential of a novel monoclonal antibody directed against antigenic site B of the hemagglutinin of influenza A viruses. PLoS Pathog. 5:e1000350