1887

Abstract

Conclusions

The secondary and tertiary structures of the rabies virus spike G protein are important for its ability to induce VN antibodies and confer immunity to the host. For a subunit peptide vaccine to be as effective as the native spike G protein, it would appear that the amino acid sequence comprising the antigenic determinant for VN antibody binding must be made to fold properly even when deprived of its native support structure. Since CNBr peptides have retained at least some of their antigenicity for binding antibodies from hyperimmune serum but not monoclonal VN antibodies, and their immunogenicity, then synthetic peptides containing corresponding sequences should show similar activities. Additionally, determinants that might be necessary for stimulating T lymphocytes would have to be built into the synthetic peptide preparation. It would also appear that a properly folded peptide might have to be aggregated into suitably large particles for it to achieve its full protective effect. Adjuvants may serve in this capacity to enhance the immune response to relevant peptides and thus improve the immunogenicity of a subunit vaccine that ultimately protects animals and humans against rabies virus infection.

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1983-08-01
2024-04-30
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References

  1. Anilionis A., Wunner W. H., Curtis P. J. 1981; Structure of the glycoprotein gene in rabies virus. Nature, London 294:275–278
    [Google Scholar]
  2. Atanasiu P., Perrin P., Delagneau J. F. 1980; Use of an enzyme immunoassay with protein A for rabies antigen and antibody determination. In Developments in Biological Standardization vol 46: pp 207–215 Edited by Regamey R. H. Basel: S. Karger;
    [Google Scholar]
  3. Atanasiu P., Perrin P., Delagneau J. F., Versmisse P., Chevallier G., Reculard P., Lefur R., Sureau P. 1982; Titrage immunoenzymatique de la glycoproteine, une technique in vitro pour l’appreciation de l’activite des vaccins antirabiques. Journal of Biological Standardization 10:289–296
    [Google Scholar]
  4. Bittle J. L., Houghton R. A., Alexander H., Shinnick T. M., Sutcliffe I. G., Lerner R. A., Rowlands D. J., Brown F. 1982; Protection against foot-and-mouth disease by immunization with a chemically synthesized peptide predicted from the viral nucleotide sequence. Nature, London 298:30–33
    [Google Scholar]
  5. Brown F., Crick J. 1974; Antibody response to subunits of rabies and vesicular stomatitis viruses. In Immunobiological Standardization vol 21: pp 114–123 Edited by Regamey R. H., Lang R., Hennessen W., Perkins F. T., Triau R. Basel: S. Karger;
    [Google Scholar]
  6. Cox J. H., Dietzschold B., Schneider L. G. 1977; Rabies virus glycoprotein. II. Biological and serological characterization. Infection and Immunity 16:754–759
    [Google Scholar]
  7. Cox J. H., Dietzschold B., Weiland F., Schneider L. G. 1980; Preparation and characterization of rabies virus hemagglutinin. Infection and Immunity 30:572–577
    [Google Scholar]
  8. Crick J., Brown F. 1969; Viral subunits for rabies vaccination. Nature, London 222:92
    [Google Scholar]
  9. Crick J., Brown F. 1970; Small immunizing subunits in rabies virus. In The Biology of the Large RNA Viruses pp 133–140 Edited by Barry R. D., Mahy B. W. J. London: Academic Press;
    [Google Scholar]
  10. Curtis P. J., Anilionis A., Wunner W. H. 1981; Cloning of full-length cDNA from the rabies virus glycoprotein gene. In The Replication of Negative Strand Viruses pp 721–725 Edited by Bishop D. H. L., Compans R. W. Amsterdam: Elsevier/North-Holland;
    [Google Scholar]
  11. Dietzschold B., Schneider L. G., Cox J. H. 1974; Serological characterization of the three major proteins of vesicular stomatitis virus. Journal of Virology 14:1–7
    [Google Scholar]
  12. Dietzschold B., Cox J. H., Schneider L. G., Wiktor T. J., Koprowski H. 1978; Isolation and purification of a polymeric form of the glycoprotein of rabies virus. Journal of General Virology 40:131–139
    [Google Scholar]
  13. Dietzschold B., Wiktor T. J., Macfarlan R., Varrichio A. 1982; Antigenic structure of rabies virus glycoprotein: ordering and immunological characterization of the large CNBr cleavage fragments. Journal of Virology 44:595–602
    [Google Scholar]
  14. Dietzschold B., Wiktor T. J., Wunner W. H., Varrichio A. 1983; Chemical and immunological analysis of the rabies soluble glycoprotein. Virology 124:330–337
    [Google Scholar]
  15. Ferguson M., Schild G. C. 1982; A single-radial-immunodiffusion technique for the assay of rabies glycoprotein antigen: application for potency tests of vaccines against rabies. Journal of General Virology 59:197–201
    [Google Scholar]
  16. Hackett C. J., Dietzschold B., Gerhard W., Ghrist B., Knorr R., Gillissen D., Melchers F. 1983; The influenza virus site recognized by a murine helper T cell specific for HI strains: localization to a nine amino acid sequence in the hemagglutinin molecule. Journal of Experimental Medicine (in press)
    [Google Scholar]
  17. Irving R. A., Ghosh H. P. 1982; Shedding of vesicular stomatitis virus soluble glycoprotein by removal of carboxy-terminal peptide. Journal of Virology 42:322–325
    [Google Scholar]
  18. Kleid D. G., Yansura D., Small B., Dowbenko D., Moore D. M., Grubman M. J., Mckercher P. D., Morgan D. O., Robertson B. H., Bachrach H. L. 1981; Cloned viral protein vaccine for foot-and-mouth disease: responses in cattle and swine. Science 214:1125–1129
    [Google Scholar]
  19. Lai C. Y., Dietzschold B. 1981; Amino acid composition and terminal sequence analysis of the rabies virus glycoprotein: identification of the reading frame on the cDNA sequence. Biochemical and Biophysical Research Communications 103:536–542
    [Google Scholar]
  20. Little S. P., Huang A. S. 1978; Shedding of the glycoprotein from vesicular stomatitis virus-infected cells. Journal of Virology 27:330–339
    [Google Scholar]
  21. Perrin P., Atanasiu P. 1981; Rabies glycoprotein affinity for lipids. I. Structural study of different types of spontaneous and induced associations. Microbiologica 4:231–247
    [Google Scholar]
  22. Sikes R. K., Clearly W. F., Koprowski H., Wiktor T. J., Kaplan M. M. 1971; Effective protection of monkeys against death by street virus by post-exposure administration of tissue-culture rabies vaccine. Bulletin of the World Health Organization 45:1–11
    [Google Scholar]
  23. Wiktor T. J. 1978; Cell-mediated immunity and post-exposure protection from rabies by inactivated vaccines of tissue culture origin. In Developments in Biological Standardization vol 40: pp 256–264 Edited by Hennessen W., Regamey R. H. Basel: S. Karger;
    [Google Scholar]
  24. Wiktor T. J., Postic B., Ho M., Koprowski H. 1972; Role of interferon induction in the protective activity of rabies vaccines. Journal of Infectious Diseases 126:408–418
    [Google Scholar]
  25. Wiktor T. J., György E., Schlumberger H. D., Sokol F., Koprowski H. 1973; Antigenic properties of rabies virus components. Journal of Immunology 110:269–276
    [Google Scholar]
  26. Wiktor T. I., Koprowski H., Mitchell J. R., Merigan T. C. 1976; Role of interferon in prophylaxis of rabies after exposure. Journal of Infectious Diseases 133:A260–A265
    [Google Scholar]
  27. Wiktor T. J., Doherty P. C., Koprowski H. 1977; In vitro evidence of cell-mediated immunity after exposure of mice to both live and inactivated rabies virus. Proceedings of the National Academy of Sciences, U. S. A 74:334–338
    [Google Scholar]
  28. Yelverton E., Norton S., Obijeski J. F., Goeddel D. V. 1983; Rabies virus glycoprotein analogs: biosynthesis in Escherichia coli. Science 219:614–620
    [Google Scholar]
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