Glycosylation of vesicular stomatitis virus glycoprotein in virus-infected HeLa cells.
Glycosylation of the envelope glycoprotein of vesicular stomatitis virus was examined using virus-infected HeLa cells that were pulse-labeled with radioactive sugar precursors. The intracellular sites of glycosylation and the stepwise elongation of the carbohydrate side chains of the G protein were monitored by membrane fractionation and gel filtration of Pronase-digested glycopeptides. The results with short pulses of sugar label (5 to 10 mtein linkage (glucosamine and mannose) are added to G which was associated with the rough endoplasmic reticulum-enriched membrane fraction, whereas the more distal sugars (galactose, sialic acid, fucose, and possibly more glucosamine) are added in the light-density internal membrane fraction. Accumulation of mature G was observed in the plasma membrane-enriched fraction. The gel filtration studies indicated that the initial glycosylation event may be the en bloc addition of a mannose and glucosamine oligomer, followed by the stepwise addition of the more distal sugars.
D002845:Chromatography; D002850:Chromatography, Gel; D005643:Fucose / Q000378:metabolism; D005690:Galactose / Q000378:metabolism; D005944:Glucosamine / Q000378:metabolism*; D006020:Glycopeptides / Q000032:analysis; D006023:Glycoproteins / Q000378:metabolism*; D006367:HeLa Cells; D006601:Hexoses / Q000378:metabolism*; D008358:Mannose / Q000378:metabolism; D014721:Vesicular stomatitis Indiana virus / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism*
D006020:Glycopeptides; D006023:Glycoproteins; D006601:Hexoses; D014764:Viral Proteins; D005643:Fucose; D005944:Glucosamine; D008358:Mannose; D005690:Galactose