1887

Abstract

Summary

A panel of monoclonal antibodies (MAbs) raised against an Indian strain of Japanese encephalitis (JE) virus was used to map topographically the epitopes on the envelope protein. Two separate clusters of epitopes were revealed. On the basis of reactivity in haemagglutination inhibition (HI), neutralization (NT), passive protection and antibody-dependent plaque enhancement (ADPE) assays with the MAbs, five functional domains (A, B, C, D and E) were delineated. The flavivirus cross-reactive domain for HI (A) was distinct. The JE virus-specific domain for HI (B) was in continuum with those domains representing non-HI JE virus-specific MAbs (C) and flavivirus cross-reactive MAbs (D). Domain E, which mapped close to domain D was represented by two MAbs that reacted with both JE virus and uninfected cell nuclei. Four conclusions can be drawn. (i) Two distinct antigenic domains were associated with HI, (ii) HI and NT and were dissociated functions, (iii) ADPE activity was solely linked with the A domain and (iv) all MAbs reacting with epitopes in the B domain had HI/NT/protective activity but failed to show ADPE. The B domain might therefore be considered the most suitable for development of synthetic or genetically engineered vaccines.

Keyword(s): E protein , epitope mapping and JE virus
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1988-11-01
2024-04-19
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References

  1. BARRETT A. D. T., GOULD E. A. 1986; Antibody-mediated early death in vivo after infection with yellow fever virus. Journal of General Virology 67:2539–2542
    [Google Scholar]
  2. BRANDRISS M. W., SCHLESINGER J. J., WALSH E. E., BRISELLI M. 1986; Lethal 17D yellow fever encephalitis in mice. I. Passive protection by monoclonal antibodies to the envelope proteins of 17D yellow fever and dengue 2 viruses. Journal of General Virology 67:229–234
    [Google Scholar]
  3. CAMMACK V., GOULD E. A. 1986; Topographical analysis of epitope relationships on the envelope glycoprotein of yellow fever 17D vaccine and the wild type Asibi parent virus. Virology 150:333–341
    [Google Scholar]
  4. CECILIA D., GHOSH S. N. 1988; Antibody dependent plaque enhancement with monoclonal antibodies against Japanese encephalitis virus. Indian Journal of Medical Research 87:521–523
    [Google Scholar]
  5. GOULD E. A., BUCKLEY A., BARRETT A. D. T., CAMMACK N. 1986; Neutralizing (54K) and non-neutralizing (54K and 48K) monoclonal antibodies against structural and non-structural yellow fever virus proteins confer immunity in mice. Journal of General Virology 67:591–595
    [Google Scholar]
  6. GOULD E. A., BUCKLEY A., GROEGER B. K., CANE P. A., DOENHOFF M. 1987; Immune enhancement of yellow fever virus neurovirulence for mice: studies of mechanisms involved. Journal of General Virology 68:3105–3112
    [Google Scholar]
  7. HALSTEAD S. B., CHOW J. S., MARCHETTE N. J. 1973; Immunological enhancement of dengue virus replication. Nature, London 23:24–26
    [Google Scholar]
  8. HEINZ F. X. 1986; Epitope mapping of flavivirus glycoproteins. Advances in Virus Research 31:103–168
    [Google Scholar]
  9. HEINZ F. X., BERGER R., TUMA W., KUNZ C. 1983; A topological and functional model of epitopes on the structural glycoprotein of tick-borne encephalitis virus defined by monoclonal antibodies. Virology 126:525–537
    [Google Scholar]
  10. HEINZ F. X., MANDL C, BERGER R., TUMA W., KUNZ C. 1984; Antibody-induced conformational changes result in enhanced avidity of antibodies to different antigenic sites on the tick-borne encephalitis virus glycoprotein. Virology 133:25–34
    [Google Scholar]
  11. HENCHAL E. A., MCCOWN J. M., BURKE D. S., SEGUIN M. C., BRANDT W. E. 1985; Epitopic analysis of antigenic determinants on the surface of dengue-2 virions using monoclonal antibodies. American Journal of Tropical Medicine and Hygiene 34:162–169
    [Google Scholar]
  12. KEDARNATH N., CECILIA D., SATHE P. S., GADKARI D.A.A., DANDAWATE C. N., GOVERDHAN M. K., GHOSH S. N. 1986; Monclonal antibodies against Japanese encephalitis virus. Indian Journal of Medical Research 84:125–133
    [Google Scholar]
  13. 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]
  14. KIMURA-KURODA J., YASUI K. 1986; Antigenic comparison of envelope protein E between Japanese encephalitis virus and some other flavi viruses using monoclonal antibodies. Journal of General Virology 67:2663–2672
    [Google Scholar]
  15. KOBAYASHI Y., HASEGAWA H., OYAMA T., TAMAI T., KUSABA T. 1984; Antigenic analysis of Japanese encephalitis virus by using monoclonal antibodies. Infection and Immunity 44:117–123
    [Google Scholar]
  16. KOBAYASHI Y., HASEGAWA H., YAMAGUCHI T. 1985; Studies on the antigenic structure of Japanese encephalitis virus using monoclonal antibodies. Microbiology and Immunology 29:1069
    [Google Scholar]
  17. MCADA P. C, MASON P. W., SCHMALJOHN C. S., DALRYMPLE J. M., MASON T. L., FOURNIER M. J. 1987; Partial nucleotide sequence of Japanese encephalitis virus genome. Virology 158:348–360
    [Google Scholar]
  18. MCCULLOUGH K. C. 1986; Monoclonal antibodies: implication for virology. Archives of Virology 87:1–36
    [Google Scholar]
  19. MASON P. W., MCADA P. C, DALRYMPLE J. M., FOURNIER M. J., MASON T. L. 1987; Expression of Japanese encephalitis virus antigens in. Escherichia coli. Virology 158:361–372
    [Google Scholar]
  20. MONATH T. P. 1985 Flaviviruses. Virology955–1004 Edited by Fields B. N. New York: Raven Press;
    [Google Scholar]
  21. MONATH T. P. 1986 Pathobiology of flaviviruses. The Togaviridae and Flaviviridae375–440 Edited by Schlesinger S., Schlesinger M. J. New York & London: Plenum Press;
    [Google Scholar]
  22. PORTERFIELD J. S. 1980 Antigenic characteristics and classification of Togaviridae. The Togaviruses13–46 Edited by Schlesinger R. W. New York: Academic Press;
    [Google Scholar]
  23. ROEHRIG J. T. 1986 The use of monoclonal antibodies in studies of the structural proteins of togaviruses and flaviviruses. III. Flaviviruses. The Togaviridae and Flaviviridae265–272 Edited by Schlesinger S., Schlesinger M. J. New York & London: Plenum Press;
    [Google Scholar]
  24. SCHLESINGER J. J., WALSH E. E., BRANDRISS M. W. 1984; Analysis of 17D yellow fever virus envelope protein epitopes using monoclonal antibodies. Journal of General Virology 65:1637–1644
    [Google Scholar]
  25. SCOTT R. McN., ECKELS K. H., BANCROFT W. H., SUMMERS P. L., MCCOWN J. M., ANDERSON J. H., RUSSELL P. K. 1983; Dengue-2 vaccine: dose response in volunteers in relation to yellow fever immune status. Journal of Infectious Diseases 148:1055–1060
    [Google Scholar]
  26. WESTAWAY E. G., BRINTON M. A., GAIDAMOVICH S. YA., HORZINEK M. C, IGARASHI A., KÄÄRIÄINEN L., LVOV D. K., PORTERFIELD J. S., RUSSELL P. K., TRENT D. W. 1985; Flaviviridae. Intervirology 24:183–192
    [Google Scholar]
  27. YEWDELL J. W., GERHARD W. 1981; Antigenic characterization of viruses by monoclonal antibodies. Annual Review of Microbiology 35:185–206
    [Google Scholar]
  28. YOLKEN R. H., LEISTER F. J., WHITCOMB L. S., SANTOSHAM M. 1983; Enzyme immunoassays for the detection of bacterial antigens utilizing biotin-labelled antibody and peroxidase biotin-avidin complex. Journal of Immunological Methods 56:319–327
    [Google Scholar]
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