Host cell-induced differences in the O-glycosylation of herpes simplex virus gC-1. II. Demonstration of cell-specific galactosyltransferase essential for formation of O-linked oligosaccharides.

By using a lectin-based screening method for cell-dependent variations of O-glycosylation of viral glycoprotein, we found that O-linked oligosaccharides of herpes simplex virus type 1 (HSV-1) glycoproteins in virus-infected mouse neuroblastoma (C1300) cells differed from those of HSV glycoproteins produced in other cells. Thus, O-linked oligosaccharides of HSV-1-specified glycoprotein C (gC-1), produced in GMK cells and a number of other cells, occurred mainly as trisaccharides or larger structures. In contrast, gC-1, produced in C1300 cells, contained O-linked monosaccharides and very few, if any, larger oligosaccharides of this class. A structural comparison between O-linked oligosaccharides of gC-1 from HSV-1-infected C1300 cells and from GMK cells showed that biosynthesis was interrupted prior to formation of a core disaccharide with terminal galactose, indicating a major early defect in O-glycosylation of glycoproteins in C1300 cells. A comparison of the content of galactosyltransferases between C1300 and GMK cells showed that C1300 cells lacked galactosyltransferases, including the specific enzyme engaged in formation of the core O-linked disaccharide mentioned, while other glycosyltransferases adding terminal sugars to O-linked oligosaccharides were present in equal amounts in both cell lines. These results indicated that HSV-1 is strictly dependent on host cell-specified factors for biosynthesis of O-linked oligosaccharides associated with viral glycoproteins.