Oligosaccharides of the Hazelhurst vesicular stomatitis virus glycoprotein are more extensively processed in Rous sarcoma virus-transformed baby hamster kidney cells

• Published in: Biochimica et biophysica acta Vol. 924; no. 1; pp. 175 - 184
• Main Author: Hunt, Lawrence A.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 16.04.1987; Elsevier; North-Holland
• Subjects: Animals; Avian Sarcoma Viruses - genetics; BHK cells; Biological and medical sciences; Carbohydrate Conformation; Carbohydrate Sequence; Cell Line; Cell Transformation, Neoplastic; Cricetinae; Fundamental and applied biological sciences. Psychology; Glycoprotein; Membrane Glycoproteins; Microbiology; Oligosaccharide processing; Oligosaccharides - genetics; Protein Processing, Post-Translational; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains; Rous sarcoma virus; Transformation; Vesicular stomatitis Indiana virus - genetics; Vesicular stomatitis Indiana virus - metabolism; Vesicular stomatitis virus; Viral Envelope Proteins; Viral Proteins - genetics; Virology; Virus Replication; Vesicular stomatitis virus; Transformation; SDS; BHK; RSV; Oligosaccharide processing; Glycoprotein; Rous sarcoma virus; VSV; BHK cells; Cell culture; Oncovirinae; Molecular structure; Transformed cell; Rodentia; Retroviridae; Glycoproteins; Glycosylation; BHK cell line; Host virus relation; Virus; Vertebrata; Vesiculovirus; Mammalia; Rhabdoviridae; Oncogenic virus; Type C oncovirus; Plasma membrane; Chemical composition; Hamster
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/0304-4165(87)90085-7

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- ß- N-acetylglucosaminidase H-sensitive oligosaccharide at the other. The major endoglycosidase-sensitive species were sialylated hybrid-type (NeuNAcGalGlcNAcMan 5GlcNAc 2Asn) from the transformed and neural-type (Man 5–6GlcNAc 2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°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°C the branching of the acidic-type oligosaccharides was increased in the virus released from the transformed cells versus normal cells.