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. © 1987 Springer-Verlag.
Dall'Olio F., Malagolini N., Campadelli-Fiume G., Serafini F. (1987). Glycosylation pattern of herpes simplex virus type 2 glycoprotein G from precursor species to the mature form. ARCHIVES OF VIROLOGY, 97(3-4), 237-249 [10.1007/BF01314424].
Glycosylation pattern of herpes simplex virus type 2 glycoprotein G from precursor species to the mature form
Dall'Olio F.;Malagolini N.;Campadelli-Fiume G.;Serafini F.
1987
Abstract
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. © 1987 Springer-Verlag.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
