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Effects of Glycosylation Inhibitors on the Expression of Polyalbumin Receptors by Hepatitis B Surface Antigen Produced in vitro

The Lillian and Henry M. Stratton - Hans Popper Department of Pathology, Mount Sinai School of Medicine, New York and City Hospital Center at Elmhurst, New York, New York 11373, U.S.A.

In this study we examined the role of secondary modifications in the expression of polyalbumin receptors by hepatitis B surface antigen (HBsAg) produced in vitro. Several clones isolated from 3T3 mouse fibroblasts after transfection with the hepatitis B virus genome produced HBsAg with marked variation in the expression of polyalbumin receptors. Treatment of the cells with glycosylation inhibitors (tunicamycin, glucosamine) resulted in loss of the 27 000 mol. wt. HBsAg glycopolypeptide, concomitantly with a marked increase in polyalbumin receptors. These data suggest that glycosylation regulates the activity of polyalbumin receptors associated with native HBsAg.

Keywords: HBsAg, polyalbumin, glycosylation, receptors

Received 20 March 1985; accepted 2 August 1985.