1887

Abstract

Antigenic differences between three of six equine influenza virus (H3N8) MDCK cell- and egg-derived pairs have been demonstrated using monoclonal and polyclonal antibodies. Sequencing of the haemagglutinin (HA) genes revealed amino acid changes in four of the six virus pairs. These data contrast with those for human isolates of influenza virus in that it was predominantly tissue culture-isolated equine virus and not egg-derived virus which displayed heterogeneity. Some of the molecular changes involved are located within the vicinity of the cell receptor-binding site (positions 156, 158 and 222) whereas others are in the vicinity of the HA1-HA2 cleavage site (positions 18 and 32 of HA1 and position 12 of HA2). Our results indicate that the host cell can play a part in selecting antigenic variants of equine influenza virus and suggest that the egg, and not cell culture as is the case for human isolates, is the preferred host for vaccine and antigenic studies.

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1994-03-01
2021-10-19
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References

  1. Cook R. F., Cook S. J. 1991; Differences in sensitivity in haemagglutinin inhibition assays between A/equine/H3N8 viruses isolated in eggs and MDCK cells are linked to cleavage of the haemagglutinin molecule. Veterinary Microbiology 27:253–261
    [Google Scholar]
  2. Cook R. F., Mumford J. A., Douglas A., Wood J. M. 1988; The influence of host cell on the antigenic properties of equine-2 influenza A viruses. In Equine Infectious Diseases V, Proceedings of the Fifth International Conference pp 6–65 Powell D. G. Edited by Lexington: University Press of Kentucky;
    [Google Scholar]
  3. Hinshaw V. S., Naeve C. W., Webster R. G., Douglas A., Skehel J. J., Bryans J. 1983; Analysis of antigenic variation in equine 2 influenza A viruses. Bulletin of the World Health Organization 61:153–158
    [Google Scholar]
  4. Katz J. M., Webster R. G. 1988; Antigenic and structural characterization of multiple subpopulations of H3N2 influenza virus from an individual. Virology 165:446–456
    [Google Scholar]
  5. Katz J. M., Webster R. G. 1989; Efficacy of inactivated influenza A virus (H3N2) vaccines grown in mammalian cells or embryonated eggs. Journal of Infectious Diseases 160:191–198
    [Google Scholar]
  6. Katz J. M., Naeve C. W., Webster R. G. 1987; Host cell mediated variation in H3N2 influenza viruses. Virology 156:386–395
    [Google Scholar]
  7. Katz J. M., Wang M., Webster R. G. 1990; Direct sequencing of the HA gene of influenza (H3N2) virus in original clinical samples reveals sequence identity with mammalian cell-grown virus. Journal of Virology 64:1808–1811
    [Google Scholar]
  8. Kawaoka Y., Webster R. G. 1989; Origin of the hemagglutinin on A/Equine/Johannesburg/86 (H3N8): the first known influenza outbreak in South Africa. Archives of Virology 106:156–164
    [Google Scholar]
  9. Oxford J. S., Corcoran T., Knott R., Bates J., Bartolomei O., Major D., Newman R. W., Yates P., Robertson J., Webster R. G., Schild G. C. 1987; Serological studies with influenza A (H1N1) viruses cultivated in eggs or in a canine kidney cell line (MDCK). Bulletin of the World Health Organization 65:181–187
    [Google Scholar]
  10. Robertson J. S., Naeve C. W., Webster R. G., Bootman J. S., Newman R., Schild G. C. 1985; Alterations in the hemagglutinin associated with adaptation of influenza B virus to growth in eggs. Virology 143:166–174
    [Google Scholar]
  11. Robertson J. S., Bootman J. S., Newman R., Oxford J. S., Daniels R. S., Webster R. G., Schild G. C. 1987; Structural changes in the hemagglutinin which accompany egg adaptation of an influenza A (H1N1) virus. Virology 160:31–37
    [Google Scholar]
  12. Robertson J. S., Bootman J. S., Nicolson C., Major D., Robertson E. W., Wood J. M. 1990; The hemagglutinin of influenza B virus present in clinical material is a single species identical to that of mammalian cell-grown virus. Virology 179:35–40
    [Google Scholar]
  13. Robertson J.S.Nicolson, Bootman J. S., Major D., Robertson E. W., Wood J. M. 1991; Sequence analysis of the haemagglutinin (HA) of influenza A (HlNl) viruses present in clinical material and comparison with the HA of laboratory-derived virus. Journal of General Virology 72:2671–2677
    [Google Scholar]
  14. Rogers A. L. 1988; A-equi-2 influenza in horses in the Republic of South Africa. Journal of the South African Veterinary Association 59:123–125
    [Google Scholar]
  15. Rott R., Orlich M., Klenk H.-D., Wang M. L., Skehel J. J., Wiley D. C. 1984; Studies on the adaptation of influenza viruses to MDCK cells. EMBO Journal 3:3329–3332
    [Google Scholar]
  16. Sanger F., Nicklen S., Coulson A. R. 1977; DNA sequencing with chain-terminating inhibitors. Proceedings of the National Academy of Sciences U.S.A.: 745463–5467
    [Google Scholar]
  17. Schild G. C., Oxford J. S., Dejong J. C., Webster R. G. 1983; Evidence for host-cell selection of influenza virus antigenic variants. Nature; London: 303706–709
    [Google Scholar]
  18. Uppal P. K., Yadav M. P., Oberoi M. S. 1989; Isolation of A/equi-2 virus during 1987 equine influenza epidemic in India. Equine Veterinary Journal 21:364–366
    [Google Scholar]
  19. Wang M., Katz J. M., Webster R. G. 1989; Extensive heterogeneity in the hemagglutinin of egg-grown influenza viruses from different patients. Virology 171:275–279
    [Google Scholar]
  20. Wiley D. C., Wilson I. A., Skehel J. J. 1981; Structural identification of the antibody binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation. Nature; London: 289373–378
    [Google Scholar]
  21. Wilson I. A., Skehel J. J., Wiley D. C. 1981; Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3A resolution. Nature; London: 289366–373
    [Google Scholar]
  22. Wood J. M., Oxford J. S., Dunleavy U., Newman R. W., Major D., Robertson J. S. 1989; Influenza A (HlNl) vaccine efficacy in animal models is influenced by two amino acid substitutions in the hemagglutinin molecule. Virology 171:214–221
    [Google Scholar]
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