1887

Abstract

To study the neutralizing epitopes of influenza B virus Victoria group strains, two monoclonal antibodies (MAbs) were used to select antigenic variants of the virus. MAbs 10B8 and 8E6 were found to react with B/Victoria group strains in three tests, peroxidase–antiperoxidase staining, haemagglutination inhibition and neutralization tests; no reactivity with B/Yamagata group strains was observed. Analysis of the deduced amino acid sequences of 10B8-induced variants identified a single amino acid deletion at residue 165 or 170, as well as a single amino acid substitution at residues 164 (Asp→Tyr), 165 (Asn→Ser or Thr) or 203 (Lys→Thr or Asn). A single amino acid substitution at residue 241 (Pro→Ser) was observed in 8E6-induced variants. Three-dimensional analysis showed that the epitopes for both MAbs were situated in close proximity to each other. Since B/Yamagata group strains are characterized by amino acid deletions at residues 164–166, the epitope for MAb 10B8 is strictly specific for B/Victoria group strains.

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2001-09-01
2020-04-03
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References

  1. Berton M. T., Webster R. G.. 1985; The antigenic structure of the influenza B virus hemagglutinin: operational and topological mapping with monoclonal antibodies. Virology143:583–594
    [Google Scholar]
  2. Berton M. T., Naeve C. W., Webster R. G.. 1984; Antigenic structure of the influenza B virus hemagglutinin: nucleotide sequence analysis of antigenic variants selected with monoclonal antibodies. Journal of Virology52:919–927
    [Google Scholar]
  3. Cleveland S. M., Taylor H. P., Dimmock N. J.. 1997; Selection of neutralizing antibody escape mutants with type A influenza virus HA-specific polyclonal antisera: possible significance for antigenic drift. Epidemiology and Infection118:149–154
    [Google Scholar]
  4. Daniels P. S., Jeffries S., Yates P., Schild G. C., Rogers G. N., Paulson J. C., Wharton S. A., Douglas A. R., Skehel J. J., Wiley D. C.. 1987; The receptor-binding and membrane-fusion properties of influenza virus variants selected using antihaemagglutinin monoclonal antibodies. EMBO Journal6:1459–1465
    [Google Scholar]
  5. Kanegae Y., Sugita S., Endo A., Ishida M., Senya S., Osako K., Nerome K., Oya A.. 1990; Evolutionary pattern of the hemagglutinin gene of influenza B viruses isolated in Japan: cocirculating lineages in the same epidemic season. Journal of Virology64:2860–2865
    [Google Scholar]
  6. Krystal M., Elliott R. M., Benz E. W. Jr, Young J. F., Palese P.. 1982; Evolution of influenza A and B viruses: conservation of structural features in the hemagglutinin genes. Proceedings of the National Academy of Sciences, USA79:4800–4804
    [Google Scholar]
  7. Lambkin R., McLain L., Jones S. E., Aldridge S. L., Dimmock N. J.. 1994; 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. Journal of General Virology75:3493–3502
    [Google Scholar]
  8. Lindstrom S. E., Hiromoto Y., Nishimura H., Saito T., Nerome R., Nerome K.. 1999; Comparative analysis of evolutionary mechanisms of the hemagglutinin and three internal protein genes of influenza B virus: multiple cocirculating lineages and frequent reassortment of the NP, M, and NS genes. Journal of Virology73:4413–4426
    [Google Scholar]
  9. Luoh S.-M., McGregor M. W., Hinshaw V. S.. 1992; Hemagglutinin mutations related to antigenic variation in H1 swine influenza viruses. Journal of Virology66:1066–1073
    [Google Scholar]
  10. McCullers J. A., Wang G. C., He S., Webster R. G.. 1999; Reassortment and insertion–deletion are strategies for the evolution of influenza B viruses in nature. Journal of Virology73:7343–7348
    [Google Scholar]
  11. Nakagawa N., Maeda A., Kase T., Kubota R., Okuno Y.. 1999; Rapid detection and identification of two lineages of influenza B strains with monoclonal antibodies. Journal of Virological Methods79:113–120
    [Google Scholar]
  12. Nakagawa N., Kubota R., Maeda A., Nakagawa T., Okuno Y.. 2000; Heterogeneity of influenza B virus strains in one epidemic season differentiated by monoclonal antibodies and nucleotide sequences. Journal of Clinical Microbiology38:3467–3469
    [Google Scholar]
  13. Nerome R., Hiromoto Y., Sugita S., Tanabe N., Ishida M., Matsumoto M., Lindstrom S. E., Takahashi T., Nerome K.. 1998; Evolutionary characteristics of influenza B virus since its first isolation in 1940: dynamic circulation of deletion and insertion mechanism. Archives of Virology143:1569–1583
    [Google Scholar]
  14. Okuno Y., Tanaka K., Baba K., Maeda A., Kunita N., Ueda S.. 1990; Rapid focus reduction neutralization test of influenza A and B viruses in microtiter system. Journal of Clinical Microbiology28:1308–1313
    [Google Scholar]
  15. Okuno Y., Isegawa Y., Sasao F., Ueda S.. 1993; A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains. Journal of Virology67:2552–2558
    [Google Scholar]
  16. Weis W., Brown J. H., Cusack S., Paulson J. C., Skehel J. J., Wiley D. C.. 1988; Structure of the influenza virus haemagglutinin completed with its receptor, sialic acid. Nature333:426–431
    [Google Scholar]
  17. Wilson I. A., Skehel J. J., Wiley D. C.. 1981; Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature289:366–373
    [Google Scholar]
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