title: Oligosaccharides of the Hazelhurst vesicular stomatitis virus glycoprotein are more extensively processed in Rous sarcoma virus-transformed baby hamster kidney cells.
abstract: Because of the extensive oligosaccharide heterogeneity of the membrane glycoprotein (G) from the Hazelhurst strain of vesicular stomatitis virus, this virus has been used as a specific intracellular probe of altered protein glycosylation in Rous sarcoma virus-transformed versus normal baby hamster kidney cells. Over 70% of G protein from virus released from the transformed cells had acidic-type oligosaccharides at both glycosylation sites, compared to less than 50% from the corresponding normal host cells. The remaining G protein contained an acidic-type oligosaccharide at one site and an endo-beta-N-acetylglucosaminidase H-sensitive oligosaccharide at the other. The major endoglycosidase-sensitive species were sialylated hybrid-type (NeuNAc-Gal-GlcNAc-Man5GlcNAc2-Asn) from the transformed and neutral-type (Man5-6GlcNAc2-Asn) from the normal host cells. The degree of branching of the acidic-type oligosaccharides was not increased in the transformed cells (approx. 80% biantennary for viral G protein from both cell types). At a reduced growth temperature (24 versus 37 degrees C), the G protein oligosaccharides were more extensively processed in both cell types (approximately 85-95% of G protein contained acidic-type structures at both sites), even though the level of viral protein synthesis and virus release was decreased. Essentially all of the minor, endoglycosidase-sensitive oligosaccharides on mature viral G protein were sialic acid-containing hybrid-type structures. At 24 degrees C the branching of the acidic-type oligosaccharides was increased in the virus released from the transformed cells versus normal cells.
mesh_terms: D000818:Animals; D001358:Avian Sarcoma Viruses / Q000235:genetics*; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002460:Cell Line; D002471:Cell Transformation, Neoplastic; D006224:Cricetinae; D008562:Membrane Glycoproteins; D009844:Oligosaccharides / Q000235:genetics*; D011499:Protein Processing, Post-Translational; D014721:Vesicular stomatitis Indiana virus / Q000235:genetics* / Q000378:metabolism; D014759:Viral Envelope Proteins; D014764:Viral Proteins / Q000235:genetics*; D014779:Virus Replication
chemical_list: C028391:G protein, vesicular stomatitis virus; D008562:Membrane Glycoproteins; D009844:Oligosaccharides; D014759:Viral Envelope Proteins; D014764:Viral Proteins