Abstract

Hepatitis B surface antigen derived from chronic hepatitis B carriers has been replaced almost completely by recombinant DNA-derived HBsAg for use as hepatitis B vaccine. Similarly, recombinant DNA-derived HBsAg is replacing plasma-derived HBsAg in standard anti-HBs assays. We analysed the influence of a change from plasma-derived HBsAg to recombinant DNA-derived HBsAg on antigen presentation in immunoassays and the characteristics of the anti-HBs antibodies after immunisation. Antigens and/or antibodies were subjected to three types of experiments: (a) binding of ‘a’-loop specific monoclonal (anti-S) antibody conjugates to immobilised vaccine-HBsAg; (b) binding of post-vaccination anti-HBs to immobilised (vaccine-)HBsAg and (c) inhibition of HBsAg binding to immobilised monoclonal anti-HBs after pre-incubation with post-vaccination antibodies. Our results show that, in both antigen presentation and anti-HBs binding properties, yeast recombinant HBsAg and related antibodies could be clearly distinguished from plasma-derived HBsAg and related antibodies. Divergent results were also obtained in the inhibition assay with recombinant DNA-derived HBsAg but not with serum HBsAg from the vaccine HBsAg subtype. It is concluded that both antigen presentation in vaccines and in anti-HBs assays can markedly influence the quantitation anti-HBs response. It is suggested that a challenge with an heterologous hepatitis B virus may encounter reduced efficacy of vaccine antibodies.

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