Identification of a dominant epitope in the hemagglutinin of an asian highly pathogenic avian influenza H5N1 clade 1 virus by selection of escape mutants

Avian Diseases

Volumn 54, Issue SUPPL. 1, 2010, Pages 565-571

  Ferreira, Helena Lage ^a   Lambrecht, Béńdicte ^a   Van Borm, Steven ^a   Torrieri Dramard, Lea ^b,c   Klatzmann, David ^b,c   Bellier, Bertrand ^b,c   Van Den Berg, Thierry ^a  

^a VETERINARY AND AGROCHEMICAL RESEARCH CENTRE   (Belgium)

^b SORBONNE UNIVERSITÉ   (France)

^c CNRS   (France)

Author keywords

Avian influenza; Hemagglutinin; Monoclonal antibody; Mutants

Indexed keywords

EPITOPE; HEMAGGLUTININ; MONOCLONAL ANTIBODY; VIRUS PROTEIN;

ASIA; CHEMICAL STRUCTURE; CHEMISTRY; CLASSIFICATION; CONFERENCE PAPER; ENZYME LINKED IMMUNOSORBENT ASSAY; GENETICS; INFLUENZA VIRUS A H5N1; METABOLISM; MUTATION; SERODIAGNOSIS;

ANTIBODIES, MONOCLONAL; ASIA; ENZYME-LINKED IMMUNOSORBENT ASSAY; EPITOPES; HEMAGGLUTININS; INFLUENZA A VIRUS, H5N1 SUBTYPE; MODELS, MOLECULAR; MUTATION; NEUTRALIZATION TESTS; VIRAL PROTEINS;

AVES; AVIAN INFLUENZA VIRUS;

EID: 77950239047     PISSN: 00052086     EISSN: None     Source Type: Journal    
DOI: 10.1637/8750-033009-ResNote.1     Document Type: Conference Paper

References (33)

1. Andersen, P. H., M. Nielsen, and O. Lund. Prediction of residues in discontinuous B cell epitopes using protein 3D structures. Protein Sci. 15:2558-2567. 2006.
2. Arnold, K., L. Bordoli, J. Kopp, and T. Schwede. The SWISSMODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22:195-201. 2006.
3. Auewarakul, P., O. Suptawiwat, A. Kongchanagul, C. Sangma, Y. Suzuki, K. Ungchusak, S. Louisirirotchanakul, H. Lerdsamran, P. Pooruk, A. Thitithanyanont, C. Pittayawonganon, C. T. Guo, H. Hiramatsu, W. Jampangern, S. Chunsutthiwat, and P. Puthavathana. An avian influenza H5N1 virus that binds to a human-type receptor. J. Virol. 81:9950-9955. 2007.
4. Ballew, H. C. Neutralization. In: Clinical virology manual. S. Specter and G. J. Lancz, eds. Elsevier, New York. pp. 187-199. 1986.
5. Baltimore, D. Expression of animal virus genomes. Bacteriol. Rev. 35:235-241. 1971.
6. Bellier, B., C. Dalba, B. Clerc, D. Desjardins, R. Drury, F. L. Cosset, M. Collins, and D. Klatzmann. DNA vaccines encoding retrovirus-based virus-like particles induce efficient immune responses without adjuvant. Vaccine 24:2643-2655. 2006.
7. Caton, A. J., G. G. Brownlee, J. M. Yewdell, and W. Gerhard. The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (H3subtype). Cell 31:417-427. 1982.
8. Council of European Communities. Council Directive 92/40/EEC of 19 May 1992 introducing community measures for the control of avian influenza. Off. J. Eur. Communities L167:1-16, 1992.
9. Desjardins, D., C. Huret, C. Dalba, F. Kreppel, S. Kochanek, F. L. Cosset, F. Tangy, D. Klatzmann, and B. Bellier. Recombinant retrovirus-like particle forming DNA vaccines in prime-boost immunization and their use for hepatitis C virus vaccine development. J. Gene Med. 26:313-325. 2009.
10. Domingo, E., and J. J. Holland. RNA virus mutations and fitness for survival. Annu. Rev. Microbiol. 51:151-178. 1997.
11. Group, World Health Organization/World Organisation for Animal Health/Food and Agricultural Organization H5N1 Evolution Working. Toward a unified nomenclature system for highly pathogenic avian influenza virus (H5N1). Emerg. Infect. Dis. 14(7), 2008. Available from: www.cdc. gov/eid/content/14/7/ e1.htm
12. Ha, Y., D. J. Stevens, J. J. Skehel, and D. C. Wiley. X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs. Proc. Natl. Acad. Sci. U. S. A. 98:11181-11186. 2001.
13. Hall, T. A. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucl. Acids Symp. Ser. 41:95-98. 1999.
14. Johansen, M. B., L. Kiemer, and S. Brunak. Analysis and prediction of mammalian protein glycation. Glycobiology 16:844-853. 2006.
15. Kamp, C. A quasispecies approach to viral evolution in the context of an adaptative immune system. Microbes Infect. 5:1397-1405. 2003.
16. Kaverin, N. V., I. A. Rudneva, E. A. Govorkova, T. A. Timofeeva, A. A. Shilov, K. S. Kochergin-Nikitsky, P. S. Krylov, and R. G. Webster. Epitope mapping of the hemagglutinin molecule of a highly pathogenic H5N1 influenza virus by using monoclonal antibodies. J. Virol. 81:12911-12917. 2007.
17. Kaverin, N. V., I. A. Rudneva, N. A. Ilyushina, A. S. Lipatov, S. Krauss, and R. G. Webster. Structural differences among hemagglutinins of influenza A virus subtypes are reflected in their antigenic architecture: analysis of H9 escape mutants. J. Virol. 78:240-249. 2004.
18. Kaverin, N. V., I. A. Rudneva, N. A. Ilyushina, N. L. Varich, A. S. Lipatov, Y. A. Smirnov, E. A. Govorkova, A. K. Gitelman, D. K. Lvov, and R. G. Webster. Structure of antigenic sites on the haemagglutinin molecule of H5 avian influenza virus and phenotypic variation of escape mutants. J. Gen. Virol. 83:2497-2505. 2002.
19. Lambkin, R., L. McLain, S. E. Jones, L. Aldridge, and N. J. Dimmock. Neutralization escape mutants of type A influenza virus are readily selected by antisera from mice immunized with whole virus: a possible mechanism for antigenic drift. J. Gen. Virol. 75:3493-3502. 1994.
20. Lambrecht, B., M. Gonze, G. Meulemans, and T. P. van den Berg. Production of antibodies against chicken interferon-g: demonstration of neutralizing activity and development of a quantitative ELISA. Vet. Immunol. Immunopathol. 74:137-144. 2000.
21. Nguyen, T. D., T. V. Nguyen, D. Vijaykrishna, R. G. Webster, Y. Guan, J. S. M. Peiris, and G. J. D. Smith. Multiple sublineages of influenza A virus (H5N1), Vietnam, 2005-2007. Emerg. Infect. Dis. 14:632-636. 2008.
22. Nielsen, M., C. Lundegaard, O. Lund, and C. Kesmir. The role of the proteasome in generating cytotoxic T cell epitopes: insights obtained from improved predictions of proteasomal cleavage. Immunogenetics 57:33-41. 2005.
23. Philpott, M., C. Hioe, M. Sheerar, and V. S. Hinshaw. Hemagglutinin mutations related to attenuation and altered cell tropism of a virulent avian influenza A virus. J. Virol. 64:2941-2947. 1990.
24. Skehel, J. J., and D. C. Wiley. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 69:531-569. 2000.
25. Steensels, M., S. Van Borm, M. Boschmans, and T. van den Berg. Lethality and molecular characterization of an HPAI H5N1 virus isolated from eagles smuggled from Thailand into Europe. Avian Dis. 51(1 Suppl):401-407. 2007.
26. Tsuchiya, E., K. Sugawara, S. Hongo, Y. Matsuzaki, Y. Muraki, Z. N. Li, and K. Nakamura. Antigenic structure of the haemagglutinin of human influenza A/H2N2 virus. J. Gen. Virol. 82:2475-2484. 2001.
27. Van Borm, S., I. Thomas, G. Hanquet, B. Lambrecht, M. Boschmans, G. Dupont, M. Decaesstecker, S. R., and T. P. van den Berg. Highly pathogenic H5N1 influenza virus isolated from eagles smuggled from Thailand into Europe. Emerg. Infect. Dis. 11:702-705. 2005.
28. Wang, J., D. Vijaykrishna, L. Duan, J. Bahl, J. X. Zhang, R. G. Webster, J. S. Peiris, H. Chen, G. J. Smith, and Y. Guan. Identification of the progenitors of Indonesian and Vietnamese avian influenza A (H5N1) viruses from southern China. J. Virol. 82:3405-3414. 2008.
29. World Health Organization (WHO) H5N1 Evolution Working Group. H5N1 nomenclature. Geneva, Switzerland; 2007. Available from: http://www.who.int/csr/ disease/avianinfluenza/guidelines/nomenclature/en/ index.html.
30. WHO. Outbreak news. Wkly. Epidemiol. Rec. 80:233-240. 2005.
31. WHO. Global Influenza Program Surveillance Program. Evolution of H5N1 avian influenza viruses in Asia. Emerg. Infect. Dis. 11:1515-1521. 2005.
32. Wiley, D. C., I. A. Wilson, and J. J. Skehel. Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation. Nature 289:373-378. 1981.
33. Wu, W. L., Y. Chen, P. Wang, W. Song, S. Y. Lau, J. M. Rayner, G. J. Smith, R. G. Webster, J. S. Peiris, T. Lin, N. Xia, Y. Guan, and H. Chen. Antigenic profile of avian H5N1 viruses in Asia from 2002 to 2007. J. Virol. 82:1798-807. 2008.