Lectin affinity chromatography of Sindbis and Rous sarcoma virus glycopeptides and oligosaccharides.
Glycopeptides and endogly cosidase-digested oligosaccharides from [3H]mannose-labeled Rous sarcoma virus and Sinbis virus have been fractionated by lentil lectin-Sepharose and concanavalin A-agarose affinity chromatography and subsequently analyzed by BioGel P-4 gel filtration. Only a specific subset of the Con A-bound asparaginly-oligosaccharides from he two viruses was also bound to lentil lectin, and this freaction apparently represented fucose-containing, diantennary acidic-type structures ((NeuNAc +/- Gal-GlcNAc)2 Man3 -GlcNAc2 (fucose)-ASN). The largest glycopeptides from Rous sarcoma virus were unbound to either Con A or lentil lectin and presumably contained tri- and/or tetra-antennary acidic-type structures ((NeuNAc +/- Gal-GlcNAc)3--4 -Man 3GlcNAc2 (+/- fucose)-ASN). In contrast, the majority of 'hybrid'-type oligosaccharides and essentially all of the neutral oligomannosyl core structures (Man5--9 GlcNAc1 and Man3 GlcNAc1) from the endoglycosidase-digested glycopeptides of both viruses were specifically bound to Con A-agarose, with the largest neutral oligosaccharides (Man7--9GlcNAc1) bound more tightly and less efficiently eluted by alpha-methyl mannoside.
D001358:Avian Sarcoma Viruses / Q000032:analysis*; D055598:Chemical Phenomena; D002621:Chemistry; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D006020:Glycopeptides / Q000302:isolation & purification*; D037102:Lectins; D009844:Oligosaccharides / Q000302:isolation & purification*; D012685:Sepharose / Q000031:analogs & derivatives; D012845:Sindbis Virus / Q000032:analysis*; D014764:Viral Proteins / Q000302:isolation & purification*
D006020:Glycopeptides; D037102:Lectins; D009844:Oligosaccharides; D014764:Viral Proteins; C028326:concanavalin A-sepharose; D012685:Sepharose