A modified hepatitis B virus surface antigen with the receptor-binding site for hepatocytes at its C terminus: expression, antigenicity and immunogenicity

The Journal of General Virology
X XuY Wang

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 PreS1 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-PreS1 antibody. A strong antibody response, against both the S protein and PreS1 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.

Citations

Aug 30, 2008·Science in China. Series C, Life Sciences·J HuiY Wang
Apr 6, 2005·World Journal of Gastroenterology : WJG·Wei-Guo HuZu-Chuan Zhang
Jun 19, 2018·Journal of Clinical Gastroenterology·Jennifer PhanSteven-Huy Han

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