1887

Abstract

The mutation rates to a viable (monoclonal antibody-resistant mutant) genotype of wild-type influenza (A/Victoria/3/75; H3N2) virus or its mutator variant strains have been previously determined. In order to estimate the mutation rates per nucleotide position, the sequence alterations present in 44 mutants isolated from either the wild-type or the 43 mutator strain have been determined. These mutants were selected with either of two non-overlapping, haemagglutinin-specific, monoclonal antibodies (2G10 and p7). Most of the protein changes were identified as substitutions of large, charged amino acids for glycine residues, as the result of G to A transitions. Particularly interesting amino acid changes, not previously reported, were observed in the p7 monoclonal antibody-specific mutants, in which only Gly to Ser and Gly to Asp at position 226 were detected. The identification of the nucleotide substitutions responsible for the phenotype has allowed the calculation of approximate values for the total mutation rates at these positions.

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1994-02-01
2024-04-25
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References

  1. Air G. M., Laver W. G. 1986; The molecular basis of antigenic variation in influenza virus. Advances in Virus Research 31:53–102
    [Google Scholar]
  2. Air G. M., Els M. C., Brown L. E., Laver W. G., Webster R. G. 1985; Location of antigenic sites on the three-dimensional structure of the influenza N2 virus neuraminidase. Virology 145:237–248
    [Google Scholar]
  3. Batschelet E., Domingo E., Weissman C. 1976; The proportion of revertant and mutant phage in a growing population as a function of mutation and growth rate. Gene 1:27–32
    [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 anti- haemagglutinin monoclonal antibodies. EMBO Journal 6:1459–1465
    [Google Scholar]
  5. Domingo E., Martínez-Salas E., Sobrino F., De La Torre J. C., Portela A., OrtíN J., López-Galindez C., Pérez-Breña P., Villanueva N., Nájera R., Vande Pol S., Steinhauer D., Depolo N., Holland J. 1985; The quasi-species (extremely heterogeneous) nature of viral RNA genome populations: biological relevance. Gene 40:1–8
    [Google Scholar]
  6. Dougherty J. P., Temin H. M. 1988; Determination of the rate of base-pair substitution and insertion mutations in retrovirus replication. Journal of Virology 62:2817–2822
    [Google Scholar]
  7. Eigen M., Schuster P. 1979 The Hypercycle. A Principle of Natural Self-organization Berlin: Springer-Verlag;
    [Google Scholar]
  8. Fields S., Winter G. 1981; Nucleotide sequence heterogeneity and sequence rearrangements in influenza virus cDNA. Gene 15:207–214
    [Google Scholar]
  9. Gallagher P., Henneberry J., Wilson I., Sambrook J., Gething M. J. 1988; Addition of carbohydrate side chains at novel sites on influenza virus hemagglutinin can modulate the folding, transport, and activity of the molecule. Journal of Cell Biology 107:2059–2073
    [Google Scholar]
  10. Holland J., Spindler K., Horodyski F., Grabau S., Nichol S., Vande Pol S. 1982; Rapid evolution of RNA genomes. Science 215:1577–1585
    [Google Scholar]
  11. Holland J. J., De La Torre J. C., Steinhauer D. A. 1992; RNA virus populations as quasispecies. Current Topics in Microbiology and Immunology 176:1–20
    [Google Scholar]
  12. Klenk H. D., Rott R. 1988; The molecular biology of influenza virus pathogenicity. Advances in Virus Research 34:247–281
    [Google Scholar]
  13. Krug R. M., Alonso-Kaplen F. V., Julkunen I., Katze M. G. 1989; Expression and replication of the influenza virus genome. In The Influenza Viruses pp. 89–152 Krug R. M. Edited by New York: Plenum Press;
    [Google Scholar]
  14. Lamb R. A. 1989; The genes and proteins of influenza viruses. In The Influenza Viruses pp. 1–87 Krug R. M. Edited by New York: Plenum Press;
    [Google Scholar]
  15. Laver W. G., Air G. M., Webster R. G., Gerhard W., Ward C. W., Dopheide T. A. 1980; The antigenic sites on influenza virus hemagglutinin. Studies on their structure and variation. In Structure and Variation in Influenza Virus pp. 295–306 Laver W. G., Air G. M. Edited by Amsterdam: Elsevier;
    [Google Scholar]
  16. Lubeck M. D., Schulman J. L., Palese P. 1980; Antigenic variants of influenza viruses: marked differences in the frequencies of variants selected with different monoclonal antibodies. Virology 102:458–462
    [Google Scholar]
  17. Luytjes W., Krystal M., Enami M., Parvin J. D., Palese P. 1989; Amplification, expression and packaging of a foreign gene by influenza virus. Cell 59:1107–1113
    [Google Scholar]
  18. Moss B. A., Underwood P. A., Bender V. J., Whittaker R. G. 1980; Antigenic drift in the hemagglutinin from various strains of influenza virus A/Hong Kong/68 (H3N2). In Structure and Variation in Influenza Virus pp. 329–338 Laver W. G., Air G. M. Edited by Amsterdam: Elsevier;
    [Google Scholar]
  19. Ortín J., Nájera R., López C., Dávila M., Domingo E. 1980; Genetic variability of Hong Kong (H3N2) influenza viruses: spontaneous mutations and their location in the viral genome. Gene 11:319–331
    [Google Scholar]
  20. Oxford J. S., Corcoran T., Schild G. C. 1980; Naturally occurring temperature-sensitive influenza A viruses of the H1N1 and H3N2 subtypes. Journal of General Virology 48:383–389
    [Google Scholar]
  21. Palese P., Young J. F. 1982; Variation of influenza A, B and C viruses. Science 215:1468–1474
    [Google Scholar]
  22. Parvin J. D., Moscona A., Pan W. T., Leider J. M., Palese P. 1986; Measurement of the mutation rates of animal viruses: influenza A virus and poliovirus type 1. Journal of Virology 59:377–383
    [Google Scholar]
  23. Portner A., Webster R. G., Bean W. H. 1980; Similar frequencies of antigenic variation in Sendai, vesicular stomatitis and influenza A viruses. Virology 104:235–238
    [Google Scholar]
  24. Rogers G. N., Paulson J. C., Daniels R. S., Skehel J. J., Wilson I. A., Wiley D. C. 1983; Single amino acid substitutions in influenza haemagglutinin change receptor binding specificity. Nature; London: 30476–78
    [Google Scholar]
  25. Steinhauer D. A., De La Torre J. C., Holland J. J. 1989; High nucleotide substitution error frequencies in clonal pools of vesicular stomatitis virus. Journal of Virology 63:2063–2071
    [Google Scholar]
  26. Suárez P., Valcárcel J., Ortín J. 1992; Heterogeneity of the mutation rate of influenza virus: isolation of mutator mutants. Journal of Virology 66:2491–2494
    [Google Scholar]
  27. Sugiura A., Tobita K., Kilbourne E. D. 1972; Isolation and preliminary characterization of temperature-sensitive mutants of influenza virus. Journal of Virology 10:639–647
    [Google Scholar]
  28. Tabor S. 1987; Exonucleases. In Current Protocols in Molecular Biology Ausubel F. M., Brent R., Kingston R. E., Moore D. D., Smith J. A., Seidman J. G., Struhl K. Edited by New York: John Wiley/Greene Publishing Associates;
    [Google Scholar]
  29. Topal M. D., Fresco J. R. 1976; Complementary base pairing and the origin of substitution mutations. Nature; London: 263285–289
    [Google Scholar]
  30. Underwood P. A., Skehel J. J., Wiley D. C. 1987; Receptorbinding characteristics of monoclonal antibody-selected antigenic variants of influenza virus. Journal of Virology 61:206–208
    [Google Scholar]
  31. Valcárcel J., Ortín J. 1989; Phenotypic hiding: the carryover of mutations in RNA viruses as shown by detection of mar mutants in influenza virus. Journal of Virology 63:4107–4109
    [Google Scholar]
  32. Van Wyke K. L., Hinshaw V. S., Bean W. J., Webster R. G. 1980; Antigenic variation of influenza A virus nucleoprotein detected with monoclonal antibodies. Journal of Virology 35:24–30
    [Google Scholar]
  33. Webster R. G., Bean W. J., Gorman O. T., Chambers T. M., Kawaoka Y. 1992; Evolution and ecology of influenza A viruses. Microbiological Reviews 56:152–179
    [Google Scholar]
  34. Wiley D. C., Skehel J. J. 1987; The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annual Review of Biochemistry 56:365–394
    [Google Scholar]
  35. Wiley D. C., Wilson I. A., Skehel J. J. 1981; Structural identification of the antibody binding sites of the Hong Kong influenza haemagglutinin and their involvement in antigenic variation. Nature; London: 298373–378
    [Google Scholar]
  36. Yewdell J. W., Webster R. G., Gerhard W. U. 1979; Antigenic variation in three distinct determinants of an influenza type A haemagglutinin molecule. Nature; London: 279246–248
    [Google Scholar]
  37. Young J. F., Desselberger U., Palese P. 1979; Evolution of human influenza A viruses in nature: sequential mutations in the genomes of new H1N1 isolates. Cell 18:73–83
    [Google Scholar]
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