Abstract
The sequence in which sugars are added to the Sindbis virus glycoproteins was studied. Infected cells contain three glycosylated virus-specific proteins: the two virion glycoproteins and the immediate precursor to the smaller virion glycoprotein. Larger Sindbis-specific proteins are not glycosylated. The cell-associated forms of both of the virion glycoproteins contain glucosamine, mannose, galactose, and fucose. The glycosylated precursor contains only glucosamine, mannose, and some galactose. The conversion of precursor to virion protein involves both the addition of galactose and fucose and the loss of mannose. The apparent extent of glycosylation of each virus-specific protein is not influenced by the host cell.
MeSH Terms
Amino Acids/metabolism
Animals
Carbohydrates/biosynthesis
Carbon Radioisotopes
Cell Line
Chick Embryo
Cricetinae
Electrophoresis, Polyacrylamide Gel
Fucose/metabolism
Galactose/metabolism
Glucosamine/metabolism
Glycoproteins/biosynthesis
Kidney
Mannose/metabolism
Protein Precursors/metabolism
Sindbis Virus/growth & development,metabolism
Tritium
Viral Proteins/biosynthesis
Chemicals
Amino Acids
Carbohydrates
Carbon Radioisotopes
Glycoproteins
Protein Precursors
Viral Proteins
Tritium
Fucose
Glucosamine
Mannose
Galactose
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Sefton B M
Burge B W
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11 references, click to expand
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