Sindbis envelope proteins as endogenous acceptors in reactions of guanosine diphosphate 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-Sindb...

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Bibliographic Details
Published in:The Journal of biological chemistry 1977-04, Vol.252 (8), p.2621-2629
Main Authors: Krag, S.S, Robbins, P.W
Format: Article
Language:English
Subjects:
Animals
Anti-Bacterial Agents - pharmacology
carbon
Cell Membrane - metabolism
Cell Transformation, Neoplastic
Cells, Cultured
Chick Embryo
Edetic Acid - pharmacology
Fibroblasts - drug effects
Fibroblasts - metabolism
Glycolipids - biosynthesis
Glycoproteins - biosynthesis
Guanosine Diphosphate Mannose - metabolism
isotopes
Membrane Proteins - biosynthesis
Nucleoside Diphosphate Sugars - metabolism
Pronase
radionuclides
Sindbis Virus - metabolism
Viral Proteins - biosynthesis
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(17)40504-7