1887

Abstract

A modified hepatitis B virus (HBV) surface antigen, the SA-28 protein, was constructed and expressed by recombinant vaccinia virus in mammalian cells. This protein was composed of a PreSl region-derived peptide (amino acids 21 to 47) that contained the hepatocyte receptor-binding site, joined to the C terminus of the major S protein at amino acid position 223. This modified surface antigen could be efficiently assembled into particles with a density of 1·23 g/ml and could be secreted from several mammalian cell lines. The results of immunoprecipitation revealed that the SA-28 protein was recognized by both the anti-S protein antibody and the anti-PreSl antibody. A strong antibody response, against both the S protein and PreSl epitopes, was induced in BALB/c mice immunized by the SA-28 particles, indicating good immunogenicity. These results suggested that the HBV surface antigen consisting of the SA-28 protein could be a promising candidate as a new HBV vaccine with higher efficacy.

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1994-12-01
2024-04-25
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References

  1. Cheng K. C., Smith G. L., Moss B. A. 1986; Hepatitis B virus large surface protein is not secreted but is immunogenic when selectively expressed by recombinant vaccinia virus. Journal of Virology 60:337–344
    [Google Scholar]
  2. Ganem D., Varmus H. E. 1987; The molecular biology of hepatitis B virus. Annual Review of Biochemistry 56:651–693
    [Google Scholar]
  3. Heermann K. H., Goldmann U., Schwarts W., Seyffarth T., Baumgerten H., Gerlich W. H. 1984; Large surface proteins of hepatitis B virus containing PreS sequence. Journal of Virology 52:396–402
    [Google Scholar]
  4. Machein U., Nagel R., Prange R., Clemen A., Streek R. E. 1992; Deletion and insertion mutants of HBsAg particles. Archives of Virology Supplementum 4 133–136
    [Google Scholar]
  5. Mackett M., Smith G. L., Moss B. 1984; General method for the production and selection of infectious vaccinia virus recombinants expressing foreign genes. Journal of Virology 49:857–864
    [Google Scholar]
  6. Neurath A. R., Kent S. B. H., Strick N., Parker K. 1986; Identification and chemical synthesis of a host cell receptor binding site on hepatitis B virus. Cell 46:429–436
    [Google Scholar]
  7. Neurath A. R., Kent S. B. H., Strick N., Parker K., Seto B., Girard M. 1988; Design of synthetic peptides mimicking the immunologic and biologic functions of the PreSl sequence of tne hepatitis B virus envelope protein. In Vaccines 88 pp. 229–234 Ginsberg H., Brown F., Lerner R. A., Chanak R. M. Edited by New York: Cold Spring Harbor Laboratory;
    [Google Scholar]
  8. Neurath A. R., Seto B., Strick N. 1989; Antibodies to synthetic peptides from the PreSl region of the hepatitis B virus (HBV) envelope (env) protein are virus-neutralizing and protective. Vaccine 7:234–236
    [Google Scholar]
  9. Wang Y., Li Z. P., Han Y. R., Zhao K., Hu Z. H., Li H. M. 1990; A subunit vaccine for hepatitis B produced by recombinant vaccinia virus. In Vaccines 90 pp. 187–191 Brown F., Ginsberg H., Lerner R. A., Chanak R. M. Edited by New York: Cold Spring Harbor Laboratory;
    [Google Scholar]
  10. Wu X., Li G. D., Feng Z. M., Zhong W. W., Chu M. J., Wang Y., Li Z. P. 1988; Construction of a universal vector pGJP-5 for gene expression in vaccinia virus. Chinese Journal of Biochemistry and Biophysics, English Edition. 20:225–235
    [Google Scholar]
  11. Xu X., Li G. D., Kong Y. Y., Wang Y. 1995; The PreSl sequence with the receptor binding site of hepatitis B virus for hepatocytes was fused to the C-terminus of major proteins of hepatitis B surface antigen. Acta Biochimica et Biophysica Sinica 27: in press
    [Google Scholar]
  12. Yu X. M. 1991; The C-terminal half of the PreSl region is essential for the secretion of human hepatitis B virus large S protein devoid of the N-terminal retention sequence. Virology 181:386–389
    [Google Scholar]
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