Glycosidase susceptibility: a probe for the distribution of glycoprotein oligosaccharides in Sindbis virus.
Intact Sindbis virus and Triton-solubilized viral glycoprotein were treated with alpha-mannosidase and with a preparation of mixed glycosidases from Diplococcus pneumoniae to probe the accesibility of carbohydrate units on the viral surface. The products of glycosidase attack on Triton-solubilized virus showed that mose carbohydrate units of the glycoproteins are good substrates for these enzymes. The relative resistance of most of the viral oligosaccharides in intact virus particles showed that much of the carbohydrate is not accessible to glycosidases, probably because it is not exposed at the viral surface. The only completely accessible carbohydrate units on Sindbis glycoproteins were the type A oligosaccharides of E2. This differential accessibility of Sindbis oligosaccharides is discussed in relation to the organization of the viral surface.
D005643:Fucose / Q000378:metabolism; D005690:Galactose / Q000378:metabolism; D005944:Glucosamine / Q000378:metabolism; D006020:Glycopeptides / Q000032:analysis; D006023:Glycoproteins / Q000302:isolation & purification* / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006387:Hemagglutination, Viral; D008358:Mannose / Q000378:metabolism; D008361:Mannosidases / Q000378:metabolism; D008961:Models, Structural; D009844:Oligosaccharides / Q000302:isolation & purification*; D012845:Sindbis Virus / Q000378:metabolism / Q000648:ultrastructure*; D013296:Streptococcus pneumoniae / Q000201:enzymology; D014764:Viral Proteins / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism
D006020:Glycopeptides; D006023:Glycoproteins; D009844:Oligosaccharides; D014764:Viral Proteins; D005643:Fucose; D006026:Glycoside Hydrolases; D008361:Mannosidases; D005944:Glucosamine; D008358:Mannose; D005690:Galactose