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.[1]References
- Sequence analysis of lactosamine type glycans of individual membrane proteins of Semliki Forest virus. Pesonen, M. J. Gen. Virol. (1979) [Pubmed]
Annotations and hyperlinks in this abstract are from individual authors of WikiGenes or automatically generated by the WikiGenes Data Mining Engine. The abstract is from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg
