1H NMR spectroscopy of carbohydrates from the G glycoprotein of vesicular stomatitis virus grown in parental and Lec4 Chinese hamster ovary cells.
Carbohydrate moieties derived from the G glycoprotein of Vesicular Stomatitis Virus (VSV) grown in parental Chinese hamster ovary (CHO) cells and the glycosylation mutant Lec4 have been analyzed by high-field 1H NMR spectroscopy. The major glycopeptides of CHO/VSV and Lec4/VSV were purified by their ability to bind to concanavalin A-Sepharose. The carbohydrates in this fraction are of the biantennary, complex type with heterogeneity in the presence of alpha(2,3)-linked sialic acid and alpha (1,6)-linked fucose residues. A minor CHO/VSV glycopeptide fraction, which does not bind to concanavalin A-Sepharose but which binds to pea lectin-agarose, was also investigated by 1H NMR spectroscopy. These carbohydrates are complex moieties which appear to contain N-acetylglucosamine in beta(1,6) linkage. Their spectral properties are most similar to those of a triantennary complex oligosaccharide containing a 2, 6-disubstituted mannose alpha (1,6) residue. Carbohydrates of this type are not found among the glycopeptides of VSV grown in the Lec4 CHO glycosylation mutant.
D000818:Animals; D002241:Carbohydrates / Q000032:analysis*; D055598:Chemical Phenomena; D002621:Chemistry; D002846:Chromatography, Affinity; D006224:Cricetinae; D003412:Cricetulus; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006023:Glycoproteins / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008562:Membrane Glycoproteins; D010053:Ovary; D014721:Vesicular stomatitis Indiana virus / Q000254:growth & development / Q000378:metabolism*; D014759:Viral Envelope Proteins; D014764:Viral Proteins / Q000378:metabolism*; D014776:Virus Cultivation
D002241:Carbohydrates; C028391:G protein, vesicular stomatitis virus; D006023:Glycoproteins; D008562:Membrane Glycoproteins; D014759:Viral Envelope Proteins; D014764:Viral Proteins