Synthesis in animal cells of hepatitis B surface antigen particles carrying a receptor for polymerized human serum albumin.
Author(s) -
MarieLouise Michel,
Patrizia Pontisso,
Eliane Sobczak,
Y. Malpièce,
Rolf E. Streeck,
Pierre Tiollais
Publication year - 1984
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.81.24.7708
Subject(s) - chinese hamster ovary cell , hbsag , hepatitis b virus , dihydrofolate reductase , microbiology and biotechnology , virology , biology , antigen , complementary dna , antibody , asialoglycoprotein receptor , recombinant dna , hepatitis b , transfection , virus , receptor , gene , biochemistry , immunology , hepatocyte , in vitro
A recombinant plasmid (pSVS dhfr) encoding the pre-S region and the S gene of human hepatitis B virus (HBV) and murine dihydrofolate reductase (DHFR) cDNA has been used for the transfection of Chinese hamster ovary (CHO) DHFR- cells. Selection of clones resistant to methotrexate has permitted amplification of HBV sequences and an increase in production of hepatitis B surface antigen (HBsAg). HBV-specific transcripts have been characterized. The HBsAg 22-nm particles contain a receptor for polymerized human serum albumin (pHSA) and elicit in animals the synthesis of antireceptor antibodies. This property is ascribed to a 34,000-dalton polypeptide in the particles, which is most likely encoded by the S gene and part of the pre-S region. Especially because the pHSA receptor is most abundantly present on the virion and because, in hepatitis B infection, the appearance of anti-pHSA receptor antibodies seems to be a highly reliable criterion for viral clearance, the HBsAg particles obtained may constitute a particularly efficient vaccine.
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