title: Sulfated components of enveloped viruses.
abstract: The glycoproteins of several enveloped viruses, grown in a variety of cell types, are labeled with 35SO4(-2), whereas the nonglycosylated proteins are not. This was shown for the HN and F glycoproteins of SV5 and Sendai virus, the E1 and E2 glycoproteins of Sindbis virus, and for the major glycoprotein, gp69, as well as for a minor glycoprotein, gp52, of Rauscher leukemia virus. The minor glycoprotein of Rauscher leukemia virus is more highly sulfated, with a ratio of 35SO4- [3H]glucosamine about threefold greater than that of gp69. The G protein of vesicular stomatitis virus was labeled when virions were grown in the MDBK line of bovine kidney cells, although no significant incorporation of 35SO4(-2) into this protein was observed in virions grown in BHK21-F line of baby hamster kidney cells. In addition to the viral glycoproteins, sulfate was also incorporated into a heterogenous component with an electrophoretic mobility lower than that of any labeled with 35SO4(-2) and [3H]leucine, this component had a much greater 35S-3H ratio than any of the viral polypeptides and thus could not represent aggregated viral proteins. This material is believed to be a cell-derived mucopolysaccharide and can be removed from virions by treatment with hyaluronidase without affecting the amount of sulfate present on the glycoproteins.
mesh_terms: D002460:Cell Line; D005944:Glucosamine / Q000032:analysis; D006023:Glycoproteins / Q000032:analysis*; D008970:Molecular Weight; D010222:Parainfluenza Virus 1, Human / Q000032:analysis; D010252:Paramyxoviridae / Q000032:analysis; D012328:RNA Viruses / Q000032:analysis*; D011925:Rauscher Virus / Q000032:analysis; D012845:Sindbis Virus / Q000032:analysis; D013431:Sulfates / Q000032:analysis*; D014764:Viral Proteins / Q000032:analysis*
chemical_list: D006023:Glycoproteins; D013431:Sulfates; D014764:Viral Proteins; D005944:Glucosamine