Effects of glycosylation inhibitors on the expression of polyalbumin receptors by hepatitis B surface antigen produced in vitro.

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.