1887

Abstract

We have previously classified isolates from a respiratory syncytial (RS) virus epidemic into distinct lineages by restriction mapping and nucleotide sequencing of parts of the nucleocapsid protein and small hydrophobic protein genes, which are areas of the genome not considered to be under immunological pressure. This study has now been extended by the determination of the nucleotide sequences of the attachment (G) protein genes of isolates from each subgroup A lineage. Deduced amino acid identities of the G proteins ranged between 80% and 99%, corresponding closely to the previously determined relatedness of the lineages. The amino acid variability was not evenly distributed; in the extracellular part of the protein there was a sharply defined hypervariable domain which was separated from a more extended variable domain by a highly conserved region. Most nucleotide changes in the variable domains were in the first and second positions of the codon triplets. These results suggest that there may be considerable immunological pressure for change in certain areas of the G protein and this may account for the ability of this virus to reinfect individuals repeatedly. The results presented here reflect the pattern of published data comparing prototype strains of the A and B subgroups.

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1991-09-01
2024-12-13
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References

  1. Anderson L. J., Heirholzer J. C., Tsou C., Hendry R. M., Fernie B. N., Stone Y., McIntosh K. 1985; Antigenic characterization of respiratory syncytial virus strains with monoclonal antibodies. Journal of Infectious Diseases 151:626–633
    [Google Scholar]
  2. Both G. W., Sleigh M. J., Cox N. J., Kendal A. P. 1983; Antigenic drift in influenza virus H3 hemagglutinin from 1968 to 1980: multiple evolutionary pathways and sequential amino acid changes at key antigenic sites. Journal of Virology 48:52–60
    [Google Scholar]
  3. Cane P. A., Pringle C. R. 1991; Respiratory syncytial virus heterogeneity during an epidemic: analysis by limited nucleotide sequencing (SH gene) and restriction mapping (N gene). Journal of General Virology 72:349–357
    [Google Scholar]
  4. Garcia-Barreno B., Paloma C., Penas C., Delgado C., Perez-Brena P., Melero J. A. 1989; Marked differences in the antigenic structure of human respiratory syncytial virus F and G glycoproteins. Journal of Virology 63:925–932
    [Google Scholar]
  5. Garcia-Barreno B., Portela A., Delgado T., Lopez J. A., Melero J. A. 1990; Frame shift mutations as a novel mechanism for the generation of neutralization resistant mutants of human respiratory syncytial virus. EMBO Journal 12:4181–4187
    [Google Scholar]
  6. Gimenez H. B., Hardman N., Keir H. M., Cash P. 1986; Antigenic variation between respiratory syncytial virus isolates. Journal of General Virology 67:863–870
    [Google Scholar]
  7. Hendricks D. A., McIntosh K., Patterson J. L. 1988; Further characterization of the soluble form of the G glycoprotein of respiratory syncytial virus. Journal of Virology 62:2228–2233
    [Google Scholar]
  8. Higgins D. G., Sharp P. M. 1988; CLUSTAL: a package for performing multiple sequence alignment on a microcomputer. Gene 73:237–244
    [Google Scholar]
  9. Johnson P. R., Collins P. L. 1989; The 1B(NS2), lC(NSl)and N proteins of human respiratory syncytial virus (RSV) of antigenic subgroups A and B: sequence conservation and divergence within RSV genomic RNA. Journal of General Virology 70:1539–1547
    [Google Scholar]
  10. Johnson P. R., Spriggs M. K., Olmsted R. A., Collins P. L. 1987; The G glycoprotein of human respiratory syncytial viruses of subgroups A and B: extensive sequence divergence between antigenically related proteins. Proceedings of the National Academy of Sciences, U S,. A. 84:5625–5629
    [Google Scholar]
  11. Kumar A., Lindberg U. 1972; Characterization of messenger ribonucleoprotein and messenger RNA from KB cells. Proceedings of the National Academy of Sciences, U.S.A. 69:681–685
    [Google Scholar]
  12. Morgan L. A., Routledge E. G., Willcocks M. M., Samson A. C. R., Scott R., Toms G. L. 1987; Strain variation of respiratory syncytial virus. Journal of General Virology 68:2781–2788
    [Google Scholar]
  13. Mufson M. A., Örvell C., Rafnar B., Norrby E. 1985; Two distinct subtypes of respiratory syncytial virus. Journal of General Virology 66:2111–2124
    [Google Scholar]
  14. Norrby E., Mufson M. A., Alexander H., Hougthen R. A., Lerner R. A. 1987; Site-directed serology with synthetic peptides representing the large glycoprotein G of respiratory syncytial virus. Proceedings of the National Academy of Sciences, U.S.A. 84:6572–6576
    [Google Scholar]
  15. Olmsted R. A., Murphy B. R., Lawrence L. A., Elango N., Moss B., Collins P. L. 1989; Processing, surface expression, and immunogenicity of carboxy-terminally truncated mutants of G protein of human respiratory syncytial virus. Journal of Virology 63:411–420
    [Google Scholar]
  16. örvell C., Norrby E., Mufson M. A. 1987; Preparation and characterization of monoclonal antibodies directed against five structural components of human respiratory syncytial virus subgroup B. Journal of General Virology 68:3125–3135.
    [Google Scholar]
  17. Palomo C., Garcia-Barreno B., Penas C., Melero J. A. 1991; The G protein of human respiratory syncytial virus: significance of carbohydrate side-chains and the C-terminal end to its antigenicity. Journal of General Virology 72:669–675
    [Google Scholar]
  18. Skehel J. J., Stevens D. J., Daniels R. S., Douglas A. R., Knossow M., Wilson I. A., Wiley D. C. 1984; A carbohydrate side chain on hemagglutinins of Hong Kong influenza viruses inhibits recognition by a monoclonal antibody. Proceedings of the National Academy of Sciences, U.S.A 81:1779–1783
    [Google Scholar]
  19. Smith F. I., Palese P. 1989; Variation in influenza virus genes: epidemiological, pathogenic, and evolutionary consequences. In The Influenza Viruses pp 319–359 Edited by Klug R. M. New York & London: Plenum Press;
    [Google Scholar]
  20. Storch G. A., Park C. S. 1987; Monoclonal antibodies demonstrate heterogeneity in the G glycoprotein of prototype strains and clinical isolates of respiratory syncytial virus. Journal of Medical Virology 22:345–356
    [Google Scholar]
  21. Sullender W. M., Anderson K., Wertz G. W. 1990; The respiratory syncytial virus subgroup B attachment glycoprotein: analysis of sequence, expression from a recombinant vector, and evaluation as an immunogen against homologous and heterologous subgroup virus challenge. Virology 178:195–203
    [Google Scholar]
  22. Wertz G. W., Collins P. L., Huang Y., Gruber C., Levine S., Ball A. L. 1985; Nucleotide sequence of the G protein gene of human respiratory syncytial virus reveals an unusual type of viral membrane protein. Proceedings of the National Academy of Sciences, U.S.A. 82:4075–4079
    [Google Scholar]
  23. Wiley D. C., Wilson I. A., Skehel J. J. 1981; Structural identification of the antibody-binding sites of Hong Kong influenza hemagglutinin and their involvement in antigenic variation. Nature, London 289:373–378
    [Google Scholar]
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