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J Gen Virol 73 (1992), 1401-1407; DOI 10.1099/0022-1317-73-6-1401
© 1992 Society for General Microbiology
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Processing of hepatitis B virus surface antigen expressed by recombinant Oka varicella vaccine virus

Kimiyasu Shiraki1, Hiroshi Ochiai1, Shoko Matsui1, Nobuyasu Aiba1, Yoshihiro Yoshida1, Toshiomi Okuno2, Koichi Yamanishi2 and Michiaki Takahashi2

1 Department of Virology, Toyama Medical and Pharmaceutical University, 2630 Sugitani, Toyama 930-01
and2 Department of Virology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565, Japan

We have constructed a recombinant Oka varicella vaccine virus expressing hepatitis B virus (HBV) surface antigen (HBsAg). HBsAg was synthesized as 26K and 30K proteins in infected cells and secreted into the culture supernatant as 30K and 35K proteins. Inhibitors and glycosidase treatments, and pulse-chase labelling experiments, revealed the glycosylation process of HBsAg. The latter was synthesized as a non-glycosylated 26K protein and subjected to N-linked glycosylation to form a 30K protein with high mannose glycans. Three species of dimers composed of 26K and 30K subunits were then formed with disulphide bonds. Both subunits of the dimers were further subjected to O-linked glycosylation and conversion from high mannose glycans to complex glycans followed by sialylation. Three species of dimers composed of 30K and 35K subunits were secreted into the culture supernatant as HBsAg particles. HBsAg was synthesized, glycosylated with both N- and O-linked glycans, sialylated, and then secreted into the culture supernatant within 1 h. These modifications of HBsAg by glycans might stabilize its structure and enhance its immunogenicity as a live HBV vaccine.

Received 26 November 1991; accepted 17 February 1992.


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