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. 1987 Apr;61(4):1286–1290. doi: 10.1128/jvi.61.4.1286-1290.1987

Selective synthesis and secretion of particles composed of the hepatitis B virus middle surface protein directed by a recombinant vaccinia virus: induction of antibodies to pre-S and S epitopes.

K C Cheng, B Moss
PMCID: PMC254096  PMID: 2434666

Abstract

Selective synthesis in mammalian cells of the hepatitis B virus middle surface (MS) protein, which is 55 amino acids longer than the major surface (S) protein, was achieved by using a recombinant vaccinia virus. The 33-kilodalton MS polypeptide was glycosylated and secreted as particles that resembled human hepatitis B surface antigen as well as particles composed solely of S protein with regard to antigenicity, buoyant density, size, and electron micrographic appearance. The MS particles differed from S particles, however, by binding to polymerized human albumin and inducing antibodies that reacted with a pre-S peptide and inhibited the binding of human plasma-derived hepatitis B surface antigen to polymerized human albumin.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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