Comparison of the oligosaccharide structure of the glycoprotein of vesicular stomatitis virus and a thermolabile mutant (tl-17).
As a means of examining the extent to which the polypeptide structure of a virus glycoprotein contributes to the overall structure and composition of the carbohydrate moieties, we have made a detailed comparison of the structure of the oligosaccharide moieties of wild-type vesicular stomatitis virus (VSV) glycoprotein with those of a glycoprotein-defective mutant of VSV, tl-17 (VSV). Characterization of the oligosaccharides by ion-exchange and gel filtration chromatography after sequential enzymic degradation reveals similar structures in the wt and mutant glycoproteins. However, the altered polypeptide structure of the tl-17 glycoprotein affects the extent of addition of sialic acid and fucose, both of which are added late in the maturation of the glycoprotein.
D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D006023:Glycoproteins / Q000032:analysis*; D009154:Mutation; D009844:Oligosaccharides / Q000032:analysis*; D011499:Protein Processing, Post-Translational; D013696:Temperature; D014721:Vesicular stomatitis Indiana virus / Q000032:analysis* / Q000235:genetics; D014759:Viral Envelope Proteins; D014764:Viral Proteins / Q000032:analysis*
D006023:Glycoproteins; D009844:Oligosaccharides; D014759:Viral Envelope Proteins; D014764:Viral Proteins