Sindbis envelope proteins as endogenous acceptors in reactions of guanosine diphosphate-[14C]Mannose with preparations of infected chicken embryo fibroblasts.
Preparations of Sindbis-infected chicken embryo fibroblasts incubated with GDP-[14C]mannose and UDP-N-acetylglucosamine catalyze the glycosylation of endogenous phospholipids and membrane-associated proteins. The proteins are identified as the viral envelope proteins by precipitation with anti-Sindbis antiserum, by comparison with authentic virion glycoproteins on sodium dodecyl sulfate-poly-acrylamide gel electrophoresis, and by comparison of the glycopeptides of the membrane-associated glycoproteins with the glycopeptides from Sindbis virions on gel filtration chromatography. Our results indicate that glycophospholipid participates in the mannosylation of the viral proteins since an inhibitor of oligosaccharide-lipid synthesis also inhibits the labeling of the glycoproteins.
D000818:Animals; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D002462:Cell Membrane / Q000378:metabolism; D002471:Cell Transformation, Neoplastic; D002478:Cells, Cultured; D002642:Chick Embryo; D004492:Edetic Acid / Q000494:pharmacology; D005347:Fibroblasts / Q000187:drug effects / Q000378:metabolism; D006017:Glycolipids / Q000096:biosynthesis; D006023:Glycoproteins / Q000096:biosynthesis; D006155:Guanosine Diphosphate Mannose / Q000378:metabolism*; D008565:Membrane Proteins / Q000096:biosynthesis*; D009702:Nucleoside Diphosphate Sugars / Q000378:metabolism*; D011402:Pronase; D012845:Sindbis Virus / Q000378:metabolism*; D014764:Viral Proteins / Q000096:biosynthesis*
D000900:Anti-Bacterial Agents; D006017:Glycolipids; D006023:Glycoproteins; D008565:Membrane Proteins; D009702:Nucleoside Diphosphate Sugars; D014764:Viral Proteins; D006155:Guanosine Diphosphate Mannose; D004492:Edetic Acid; D011402:Pronase