TY - JOUR
T1 - 1H NMR spectroscopy of carbohydrates from the G glycoprotein of vesicular stomatitis virus grown in parental and Lec4 Chinese hamster ovary cells
AU - Stanley, Pamela
AU - Vivona, Grace
AU - Atkinson, Paul H.
N1 - Funding Information:
This work was supportedb y the American Cancer Society Grant BC-322-B to P.S. and Grant CA13402-11 from the National Institutes of Health to P.H.A. Additional support was provided by the Core Cancer Grant (1POl CA 13330).P .S. is the recipient of an American Cancer Society Faculty Award. The use of the NSF Northeast Regional NMR facility at Yale University (Grant CHE-7916210)a nd the Mid-Atlantic NMR facility at the University of Pennsylvania are gratefully acknowledgedT. hanks are extendedt o Johannes Vliegenthart,J eremy Carver, and Christine Campbell for helpful discussionso r for commentso n the manuscript.
PY - 1984/4
Y1 - 1984/4
N2 - 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 α(2,3)-linked sialic acid and α(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 β(1,6) linkage. Their spectral properties are most similar to those of a triantennary complex oligosaccharide containing a 2,6-disubstituted mannose α(1,6) residue. Carbohydrates of this type are not found among the glycopeptides of VSV grown in the Lec4 CHO glycosylation mutant.
AB - 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 α(2,3)-linked sialic acid and α(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 β(1,6) linkage. Their spectral properties are most similar to those of a triantennary complex oligosaccharide containing a 2,6-disubstituted mannose α(1,6) residue. Carbohydrates of this type are not found among the glycopeptides of VSV grown in the Lec4 CHO glycosylation mutant.
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U2 - 10.1016/0003-9861(84)90119-X
DO - 10.1016/0003-9861(84)90119-X
M3 - Article
C2 - 6324683
AN - SCOPUS:0021416355
SN - 0003-9861
VL - 230
SP - 363
EP - 374
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
IS - 1
ER -