Glycopeptides of murine leukemia viruses. II. Comparison of xenotropic and dual-tropic viruses.
The glycosylation patterns of the gp70 glycoproteins of xenotropic and dualtropic murine leukemia virus (MuLV) were compared with those of ecotropic viruses. Ecotropic viruses contain a large glycopeptide size class designated G1 (molecular weight, approximately 5100), and such glycopeptides were not detected in xenotropic viruses grown in mink cells nor in dual-tropic viruses grown in mouse or mink lung cells. Both xenotropic and dual-tropic MuLV had glycopeptide size classes designated G2, G3, and G4 (molecular weights, approximately 2900, 2,200, and 1,500, respectively). G2 glycopeptides of xenotropic and dual-tropic MuLV were shown to be resistant to endo-beta-N-acetylglucosaminidase H, whereas G3 and G4 glycopeptides were susceptible. The relative abudance of glycopeptide G3 was increased in xenotropic and dual-tropic viruses as compared with ecotropic viruses, whereas the relative amount of G4 was decreased in xenotropic viruses. The similarity in the glycosylation patterns of a number of xenotropic and dual-tropic viruses suggests that glycosylation sites are highly conserved within the env gene products of each of these classes of viruses.
D000118:Acetylglucosaminidase / Q000494:pharmacology; D000818:Animals; D002460:Cell Line; D003588:Cytopathogenic Effect, Viral; D006020:Glycopeptides / Q000032:analysis*; D009052:Leukemia Virus, Murine / Q000032:analysis* / Q000254:growth & development; D051379:Mice; D008907:Mink; D008970:Molecular Weight; D013045:Species Specificity; D014764:Viral Proteins / Q000032:analysis*
D006020:Glycopeptides; D014764:Viral Proteins; D000118:Acetylglucosaminidase