Vesicular stomatitis virus G proteins with altered glycosylation sites display temperature-sensitive intracellular transport and are subject to aberrant intermolecular disulfide bonding

• Published in: The Journal of biological chemistry Vol. 263; no. 12; pp. 5955 - 5960
• Main Authors: Machamer, C E, Rose, J K
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Elsevier Inc 25.04.1988; American Society for Biochemistry and Molecular Biology
• Subjects: Binding Sites; Biological and medical sciences; Biological Transport; Cell Line; Cell Membrane - metabolism; Disulfides - metabolism; DNA, Recombinant; Endoplasmic Reticulum - metabolism; Fluorescent Antibody Technique; Fundamental and applied biological sciences. Psychology; Glycosylation; Hexosaminidases - pharmacology; Immunosorbent Techniques; Iodine Radioisotopes - metabolism; Lactoperoxidase - metabolism; Membrane Glycoproteins - metabolism; Microbiology; Mutation; Oligosaccharides - metabolism; Protein Conformation; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains; Structure-Activity Relationship; Temperature; Transfection; Vesicular stomatitis Indiana virus; vesicular stomatitis virus; Viral Envelope Proteins; Viral Matrix Proteins - genetics; Viral Matrix Proteins - metabolism; Virology; Virus; Intracellular transport; Vesicular stomatitis virus; Vesiculovirus; Rhabdoviridae; Plasma membrane; Virus replication cycle; Glycosylation; Property structure relationship; Gene expression
• DOI: 10.1016/S0021-9258(18)60659-3
• ISSN: 0021-9258

In this report we have extended our studies on a panel of vesicular stomatitis virus G proteins with altered glycosylation sites. These mutant proteins were generated by oligonucleotide-directed mutagenesis of the coding sequence to create new consensus sites for asparagine-linked oligosaccharide addition. We report that the intracellular transport of most of the mutant proteins is temperature-sensitive, implying a polypeptide folding step is affected. In addition, we find that the nonglycosylated G protein and those mutant proteins which lack oligosaccharides at the normal positions are subject to aberrant intermolecular disulfide bonding, leading to the accumulation of large complexes in the endoplasmic reticulum. These results imply that carbohydrate plays an indirect role in the intracellular transport of G protein.