Glycosylation pattern of herpes simplex virus type 2 glycoprotein G from precursor species to the mature form.

The changes in the apparent molecular weight of herpes simplex virus type 2 glycoprotein G (gG2) were studied by using different [3H] mannose labeling time intervals. Various size classes of precursors, probably derived from proteolytic cleavage of the translational product, were identified. Our experiments provide evidence that only the 74 Kd species is the real precursor of the mature 120 Kd gG2. The increase in size is due for the most part to the assembly of O-linked oligosaccharides and to a lesser extent to the conversion of N-linked chains to fucosylated diantennary species.