Sequence analysis of lactosamine type glycans of individual membrane proteins of Semliki Forest virus.
3H-fucose and 14C-glucosamine labelled glycopeptides of the individual membrane proteins E1, E2 and E3 of Semliki Forest virus could be sequentially digested with alpha-neuraminidase, beta-galactosidase, N-acetyl-beta-glucosaminidase, alpha- and beta-mannosidase, N-acetyl-beta-hexosaminidase and finally with alpha-fucosidase. The degradations of the virus glycopeptides proceeded in the same way as stepwise digestions of reference glycopeptides of the lactosamine type obtained from IgG and alpha 1-acid glycoprotein. This suggests that all three membrane glycoproteins of Semliki Forest virus contained glycans with a monosaccharide sequence characteristic for lactosamine type oligosaccharides. The number of both distal and proximal N-acetyl-glucosamine residues was estimated to be usually two. According to exo- and endo-glycosidase digestions, fucose seemed to be attached to the innermost N-acetyl-glucosamine unit.
D000117:Acetylglucosamine / Q000032:analysis; D002236:Carbohydrate Conformation; D005643:Fucose / Q000032:analysis; D005690:Galactose / Q000032:analysis; D006020:Glycopeptides / Q000032:analysis; D006026:Glycoside Hydrolases / Q000378:metabolism; D006595:Hexosamines / Q000032:analysis*; D008358:Mannose / Q000032:analysis; D008565:Membrane Proteins / Q000032:analysis*; D011134:Polysaccharides / Q000032:analysis*; D011489:Protein Denaturation; D012672:Semliki forest virus / Q000032:analysis*; D012794:Sialic Acids / Q000032:analysis; D014764:Viral Proteins / Q000032:analysis*
D006020:Glycopeptides; D006595:Hexosamines; D008565:Membrane Proteins; D011134:Polysaccharides; D012794:Sialic Acids; D014764:Viral Proteins; D005643:Fucose; D006026:Glycoside Hydrolases; D008358:Mannose; D000117:Acetylglucosamine; D005690:Galactose