The progeny of Herpes simplex virus type 1 (HSV-1) grown in ricin-resistant 14 cells (RicR14) lacking N-acetylglucosaminyltransferase I was released in the extracellular medium at a very low rate. By using a monoclonal antibody immobilized on Sepharose we purified from HSV-1-infected RicR14 cells a viral glycoprotein (gC), which carries both N-and O-linked oligosaccharides. Glycopeptides obtained from [3H]mannoselabeled gC by Pronase digestion were entirely susceptible to endo-β-N-acetylglucosaminidase H, and the major oligosaccharide released was Man4GlcNAc. The accumulation of this high-mannose species was related to the enzymic defect of the host cells and to the long retention of the viral glycoprotein within the cells. The extent of O-glycosylation evaluated in [14C]glucosamine-labeled gC from RicR14 cells as compared to that of gC from wild type cells did not appear to be significantly modified. © 1986 Glycoconjugate Journal.
Dall'Olio F., Malagolini N., Campadelli-Fiume G., Serafini F. (1986). N-and O-glycosylation of glycoprotein C synthesized by Herpes simplex virus type 1-infected ricin resistant cells. GLYCOCONJUGATE JOURNAL, 3(1), 71-84 [10.1007/BF01108613].
N-and O-glycosylation of glycoprotein C synthesized by Herpes simplex virus type 1-infected ricin resistant cells
Dall'Olio F.;Malagolini N.;Campadelli-Fiume G.;Serafini F.
1986
Abstract
The progeny of Herpes simplex virus type 1 (HSV-1) grown in ricin-resistant 14 cells (RicR14) lacking N-acetylglucosaminyltransferase I was released in the extracellular medium at a very low rate. By using a monoclonal antibody immobilized on Sepharose we purified from HSV-1-infected RicR14 cells a viral glycoprotein (gC), which carries both N-and O-linked oligosaccharides. Glycopeptides obtained from [3H]mannoselabeled gC by Pronase digestion were entirely susceptible to endo-β-N-acetylglucosaminidase H, and the major oligosaccharide released was Man4GlcNAc. The accumulation of this high-mannose species was related to the enzymic defect of the host cells and to the long retention of the viral glycoprotein within the cells. The extent of O-glycosylation evaluated in [14C]glucosamine-labeled gC from RicR14 cells as compared to that of gC from wild type cells did not appear to be significantly modified. © 1986 Glycoconjugate Journal.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
