1887

Abstract

Summary

In our previous study, seven monoclonal antibodies specific for influenza C virus glycoprotein (gp88) were prepared and tentatively classified into two groups: group A (J14, J9, Q5, K16) has neutralization activity whereas group B (S16, J6, J15) does not. These antibodies were used to analyse the antigenic structure of gp88 and to examine the effect of glycosylation on the antigenicity of the glycoprotein. Operational analysis with a panel of antigenic variants selected with each of the group A antibodies identified two non-overlapping antigenic sites on the gp88 molecules, site A-1 recognized by J14, J9 and Q5 and site A-2 by K16. Sites A-1 and A-2 were shown, however, to be topographically overlapping by competitive binding assays. Competitive binding analysis with group B antibodies identified two additional non-overlapping antigenic sites, site B-1 recognized by S16 and site B-2 by J6 and J15. It was found in radioimmunoprecipitation experiments that antibodies to sites B-1 and B-2 were reactive not only with gp88 but with its non-glycosylated form (T76) synthesized in the presence of tunicamycin. Antibodies to sites A-1 and A-2, in contrast, immunoprecipitated the T76 polypeptide in only trace amounts or not at all. Additionally, Western blot analysis showed that denatured gp88 blotted on nitrocellulose was reactive with antibodies to sites B-1 and B-2 but not with those to sites A-1 and A-2. These observations suggest that glycosylation of gp88 selectively influences the integrity of antigenic sites A-1 and A-2 which are composed of conformation-dependent epitopes.

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1988-03-01
2022-05-28
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References

  1. BERTON M. T., WEBSTER R. G. 1985; The antigenic structure of influenza B virus hemagglutinin: operational and topological mapping with monoclonal antibodies. Virology 143:583–594
    [Google Scholar]
  2. BRUCK C., RENSONNET N., PORTETELLE D., CLEUTER Y., MAMMERICKX M., BURNY A., MAMOUN R., GUILLEMAIN B., VAN DER MAATEN M. J., GHYSDAEL J. 1984; Biologically active epitopes of bovine leukemia virus glycoprotein GP51: their dependence on protein glycosylation and genetic variability. Virology 136:20–31
    [Google Scholar]
  3. BUONAGURIO D. A., NAKADA S., DESSELBERGER U., KRYSTAL M., PALESE P. 1985; Noncumulative sequence changes in the hemagglutinin genes of influenza C virus isolates. Virology 146:221–232
    [Google Scholar]
  4. CHAKRAVERTY P. 1978; Antigenic relationship between influenza C viruses. Archives of Virology 58:341–348
    [Google Scholar]
  5. COMPANS R. W., KLENK H.-D., CALLGUIRI L. A., CHOPPIN P. W. 1970; Influenza virus proteins. I. Analysis of polypeptides of the virion and identification of spike glycoproteins. Virology 42:880–889
    [Google Scholar]
  6. GUO Y. J., DESSELBERGER U. 1984; Genome analysis of influenza C viruses isolated in 1981/82 from pigs in China. Journal of General Virology 65:1857–1872
    [Google Scholar]
  7. HERRLER G., COMPANS R. W., MEIER-EWERT H. 1979; A precursor glycoprotein in influenza C virus. Virology 99:49–56
    [Google Scholar]
  8. HERRLER G., NAGELE A., MEIER-EWERT H., BHOWN A. A., COMPANS R. W. 1981; Isolation and structural analysis of influenza C glycoproteins. Virology 113:439–451
    [Google Scholar]
  9. HOMMA M., OHYAMA S., KATAGIRI S. 1982; Age distribution of the antibody to type C influenza virus. Microbiology and Immunology 26:639–642
    [Google Scholar]
  10. HONGO S., SUGAWARA K., HOMMA M., NAKAMURA K. 1986a; The functions of oligosaccharide chains associated with influenza C viral glycoproteins. I. The formation of influenza C virus particles in the absence of glycosylation. Archives of Virology 89:171–187
    [Google Scholar]
  11. HONGO S., SUGAWARA K., HOMMA M., NAKAMURA K. 1986b; The functions of oligosaccharide chains associated with influenza C viral glycoproteins. II. The role of carbohydrates in the antigenic properties of influenza C viral glycoproteins. Archives of Virology 89:188–201
    [Google Scholar]
  12. JENNINGS R. 1968; Respiratory viruses in Jamaica: a virologie and serologic study. 3. Hemagglutination-inhibiting antibodies to type B and C influenza viruses in the sera of Jamaicans. American Journal of Epidemiology 87:440–445
    [Google Scholar]
  13. KATAGIRI S., OHIZUMI A., HOMMA M. 1983; An outbreak of type C influenza in a children’s home. Journal of Infectious Diseases 148:51–55
    [Google Scholar]
  14. KAWAMURA H., TASHIRO M., KITAME F., HOMMA M., NAKAMURA K. 1986; Genetic variation among human strains of influenza C virus isolated in Japan. Virus Research 4:275–288
    [Google Scholar]
  15. KIDA H., BROWN L. E., WEBSTER R. G. 1982; Biological activity of monoclonal antibodies to operationally defined antigenic regions on the hemagglutinin molecule of A/seal/Massachusetts/1/80 (H7N7) influenza virus. Virology 122:38–47
    [Google Scholar]
  16. KIMURA-KURODA J., YASUI K. 1983; Topographical analysis of antigenic determinants on envelope glycoprotein V3(E) of Japanese encephalitis virus, using monoclonal antibodies. Journal of Virology 45:124–132
    [Google Scholar]
  17. LONG L., PORTETELLE D., GHYSDAEL J., GONZE M., BURNY A., MEULEMANS G. 1986; Monoclonal antibodies to hemagglutinin-neuraminidase and fusion glycoproteins of Newcastle disease virus: relationship between glycosylation and reactivity. Journal of Virology 57:1198–1202
    [Google Scholar]
  18. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. 1951; Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193:265–275
    [Google Scholar]
  19. MEIER-EWERT H., PETRI T., BISHOP D. H. L. 1981; Oligonucleotide fingerprint analyses of influenza C virion RNA recovered from five different isolates. Archives of Virology 67:141–147
    [Google Scholar]
  20. NAKADA S., CREAGER R. S., KRYSTAL M., AARONSON R. P., PALESE P. 1984; Influenza C virus hemagglutinin: comparison with influenza A and B virus hemagglutinins. Journal of Virology 50:118–124
    [Google Scholar]
  21. NEROME K., ISHIDA M., NAKAYAMA M. 1979; Established cell line sensitive to influenza C virus. Journal of General Virology 43:257–259
    [Google Scholar]
  22. O’CALLAGHAN R. J., GOHD R. S., DABAT D. D. 1980; Human antibody to influenza C virus: its age-related distribution and distinction from receptor analogs. Infection and Immunity 30:500–505
    [Google Scholar]
  23. PFEIFER J. B., COMPANS R. W. 1984; Structure of the influenza C glycoprotein gene as determined from cloned DNA. Virus Research 1:281–296
    [Google Scholar]
  24. PORTNER A., WEBSTER R. G., BEAN W. J. 1980; Similar frequencies of antigenic variants in Sendai, vesicular stomatitis, and influenza A viruses. Virology 104:235–238
    [Google Scholar]
  25. SUGAWARA K., OHUCHI M., NAKAMURA K., HOMMA M. 1981; Effects of various proteases on the glycoprotein composition and the infectivity of influenza C virus. Archives of Virology 68:147–151
    [Google Scholar]
  26. SUGAWARA K., NISHIMURA H., KITAME F., NAKAMURA K. 1986; Antigenic variation among human strains of influenza C virus detected with monoclonal antibodies to gp88 glycoprotein. Virus Research 6:27–32
    [Google Scholar]
  27. TOWBIN H., STAEHELIN T., GORDON J. 1979; Electrophoretic transfer of proteins from Polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proceedings of the National Academy of Sciences, U.S.A 76:4350–4354
    [Google Scholar]
  28. WEBSTER R. G., BERTON M. T. 1981; Analysis of antigenic drift in the haemagglutinin molecule of influenza B virus with monoclonal antibodies. Journal of General Virology 54:243–251
    [Google Scholar]
  29. WEBSTER R. G., LAVER W. G. 1980; Determination of the number of nonoverlapping antigenic areas on Hong Kong (H3N2) influenza virus hemagglutinin with monoclonal antibodies and the selection of variants with potential epidemiological significance. Virology 104:139–148
    [Google Scholar]
  30. WEBSTER R. G., HINSHAW V. S., LAVER W. G. 1982; Selection and analysis of antigenic variants of the neuraminidase of N2 influenza viruses with monoclonal antibodies. Virology 117:93–104
    [Google Scholar]
  31. WILSON B. M., NAKANE P. K. 1978 Recent developments in the periodate method of conjugating horse-radish peroxidase (HRPO) to antibodies. Immunofluorescence and Related Staining Techniques215–222 Edited by Knapp W., Holubat K., Wick G. Amsterdam: Elsevier North-Holland;
    [Google Scholar]
  32. YOKOTA M., NAKAMURA K., SUGAWARA K., HOMMA M. 1983; The synthesis of polypeptides in influenza C virus-infected cells. Virology 130:105–117
    [Google Scholar]
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