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Human sera possess a limited antibody repertoire to influenza neuraminidase antigenic variants selected in vitro

Published online by Cambridge University Press:  19 October 2009

Anita Natali
Affiliation:
Institute of Microbiology, University of Parma, Italy
P. F. Panizzi
Affiliation:
Institute of Microbiology, University of Parma, Italy
C. Chezzi
Affiliation:
Institute of Microbiology, University of Parma, Italy
J. S. Oxford
Affiliation:
Division of Virology, National Institute for Biological Standards and Control, Hampstead, London NW3 6RB
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Summary

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Four antigenic variants of the neuraminidase (NA) of A/Texas/77 (H3N2) virus were selected using monoclonal antibody at a frequency of one variant in 105 parental virions. The antigenic variants failed to react serologically with the monoclonal antibody used for their selection in vitro. The antigenic variants failed also to react serologically with a proportion of sera from children and adults although all of the sera reacted with the parental A/Texas/77 virus. Thus, certain human sera have a restricted antibody repertoire to influenza NA antigen which might enable virus antigenic variants to avoid anti-NA antibody-mediated neutralization in nature.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1984

References

REFERENCES

Appleyard, G. & Oram, J. D. (1977). The assay of influenza antineuraminidase activity by an elution inhibition technique. Journal of General Virology 34, 137144.CrossRefGoogle ScholarPubMed
Aymard-Henry, M., Coleman, M. T., Dowdle, W. R., Laver, W. G., Schild, G. C. & Webster, R. G. (1973). Influenza virus neuraminidase and neuraminidase inhibition test procedures. Bulletin of the World Health Organization 48, 199202.Google ScholarPubMed
Blok, J. & Air, G. M. (1980). Comparative nucleotide sequences at the 3′ end of the neuraminidase gene from 11 influenza type A virus. Virology 107, 5060.CrossRefGoogle Scholar
Fields, S., Winter, G. & Brownlee, G. G. (1981). Structure of the neuraminidase gene in human influenza virus A/PR/8/34. Nature 290, 213217.CrossRefGoogle ScholarPubMed
Gerhard, W. & Webster, R. G. (1978). Antigenic drift in influenza A viruses. Selection and characterisation of antigenic mutants of A/PR/8/34 (NON 1) virus with monoclonal antibodies. Journal of Experimental Medicine 148, 383392.CrossRefGoogle Scholar
Haaheim, L. R. & Schild, G. C. (1976). Antigenic variants of influenza A virus obtained in vitro. Bulletin of the World Health Organization 53, 305311.Google ScholarPubMed
Inglis, S. C., Carroll, A. R., Lamb, R. A. & Mahy, B. W. J. (1976). Polypeptides specified by the influenza virus genome. Evidence for eight distinct gene products specified by fowl plague virus. Virology 74, 489503.CrossRefGoogle ScholarPubMed
Jahiel, R. I. & Kilbourne, E. D. (1966). Reduction in plaque size and reduction in plaque number as differing indices of influenza virus–antibody reactions. Journal of Bacteriology 92, 1521.CrossRefGoogle ScholarPubMed
Kilbourne, E. D., Laver, W. J., Schulman, J. L. & Webster, R. G. (1968). Antiviral activity of antiserum specific for an influenza virus neuraminidase. Journal of Virology 2, 281.CrossRefGoogle ScholarPubMed
Koprowski, H., Gerhard, W. & Crock, C. M. (1977). Production of antibodies against influenza virus by somatic cell hybrids between mouse myeloma and primed spleen cells. Proceedings of the National Academy of Science (USA) 74, 29852988.CrossRefGoogle ScholarPubMed
Laver, W. G., Gerhard, W., Webster, R. G., Frankel, M. E. & Air, G. M. (1979). Antigenic drift in type A influenza virus: peptide mapping and antigenic analysis of A/PR/8/34 (HON 1) variants selected with monoclonal antibodies. Proceediiigs of the National Academy of Science (USA) 76, 14251429.CrossRefGoogle Scholar
Natali, A., Oxford, J. S. & Schild, G. C. (1981). Frequency of naturally occurring antibody to influenza virus antigenic variants selected with monoclonal antibody. Journal of Hygiene 87, 185190.CrossRefGoogle ScholarPubMed
Natali, A., Panizzi, P. F., Conti, G. & Schito, G. C. (1982). Varianti di A/Texas/77 (H3N2) per neunaminidasi selezionate con anticorpi monoclonali: nota preliminare. Proceedings of XLI Congress T.U.E.M.A. of Italian Society of Microbiology.Google Scholar
Oxford, J. S., Corcoran, T. & Schild, G. C. (1981 b). Intratypic electrophoretic variation of structural and non-structural polypeptides of human influenza A viruses. Journal of General Virology 56, 431436.CrossRefGoogle ScholarPubMed
Oxford, J. S., Haaheim, L. R., Slepushkin, A., Werner, J., Kuwert, E. & Schild, G. C. (1981 a). Strain specificity of serum antibody to the haemagglutinin of influenza A (H3N2) viruses in children following immunization or natural infection. Journal of Hygiene 86, 1726.CrossRefGoogle ScholarPubMed
Paniker, K. J. (1968). Serological relationships between the neuraminidases of influenza viruses. Journal of General Virology 2, 385.CrossRefGoogle ScholarPubMed
Schild, G. C., Pereira, M. S., Chakraverty, P. (1975). Single-radial-haemolysis: a new method for the assay of antibody to influenza haemagglutinin. Bulletin of World Health Organization 52, 4350.Google ScholarPubMed
Seto, J. T. & Rott, R. (1966). Functional significance of sialidase during influenza virus multiplication. Virology 30, 731.CrossRefGoogle ScholarPubMed
Webster, R. G. & Laver, W. G. (1975). Antigenic variation of influenza virus. In The Influenza Virus and Influenza (ed. Kilbourne, E. D.), pp. 260314. New York: Academic Press.Google ScholarPubMed
Webster, R. G., Laver, W. G., Air, G. M. & Schild, G. C. (1982 a). Molecular mechanisms of variation in influenza viruses. Nature 296, 115121.CrossRefGoogle ScholarPubMed
Webster, R. G., Hinshaw, V. S. & Laver, W. G. (1982 b). Selection and analysis of antigenic variants of neuraminidase of N2 influenza viruses with monoclonal antibodies. Virology 117, 93104.CrossRefGoogle ScholarPubMed
Yewdell, J. W., Webster, R. G. & Gerhard, W. U. (1979). Antigenic variation in three distinct determinants of an influenze type A haemagglutinin molecule. Nature 279, 246248.CrossRefGoogle Scholar