title: Altered G-protein glycosylation in vesicular stomatitis virus-infected glucose-deprived baby hamster kidney cells.
abstract: The glycosylation of the G-protein was analyzed in vesicular stomatitis virus-infected baby hamster kidney cells incubated in the absence of glucose. The results indicate that the G-protein in glucose-starved cells is initially glycosylated from a lipid donor with a glucosylated oligosaccharide which is resistant to endo-beta-N-acetylglucosaminidase H and partially susceptible to alpha-mannosidase. With longer times, the protein-bound carbohydrate chain becomes much more sensitive to alpha-mannosidase while remaining endo-beta-N-acetylglucosaminidase H-resistant. Purified virions from glucose-starved baby hamster kidney cells, labeled with [35S]methionine and isolated on a sucrose gradient, contain altered forms of the G-protein, whereas the other viral proteins remain unchanged. These altered forms could also be radiolabeled with [3H]mannose, and upon analysis of labeled glycopeptides by chromatography on concanavalin A-Sepharose and Bio-Gel P-6, it was apparent that modification of the oligosaccharide portion of the G-protein occurs in baby hamster kidney cells, leading to aberrant mature carbohydrate chains.
mesh_terms: D000818:Animals; D002460:Cell Line; D006224:Cricetinae; D005690:Galactose / Q000378:metabolism; D005947:Glucose / Q000172:deficiency*; D007668:Kidney / Q000378:metabolism*; D008358:Mannose / Q000378:metabolism; D008562:Membrane Glycoproteins; D008715:Methionine / Q000378:metabolism; D013997:Time Factors; D014721:Vesicular stomatitis Indiana virus; D014759:Viral Envelope Proteins; D014764:Viral Proteins / Q000096:biosynthesis*; D014777:Virus Diseases / Q000378:metabolism*
chemical_list: C028391:G protein, vesicular stomatitis virus; D008562:Membrane Glycoproteins; D014759:Viral Envelope Proteins; D014764:Viral Proteins; D008715:Methionine; D005947:Glucose; D008358:Mannose; D005690:Galactose