H-fucose and C-glucosamine labelled glycopeptides of the individual membrane proteins E1, E2 and E3 of Semliki Forest virus could be sequentially digested with α-neuraminidase, β-galactosidase, -acetyl-β-glucosaminidase, α- and β-mannosidase, -acetyl-β-hexosaminidase and finally with α-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 α-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 -acetyl-glucosamine residues was estimated to be usually two. According to exo- and endo-glycosidase digestions, fucose seemed to be attached to the innermost -acetyl-glucosamine unit.


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