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

Carolyn E Machamer, J. K. Rose

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)5955-5960
Number of pages6
JournalJournal of Biological Chemistry
Volume263
Issue number12
StatePublished - 1988
Externally publishedYes

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Glycosylation
Mutant Proteins
Disulfides
Oligosaccharides
GTP-Binding Proteins
Temperature
Mutagenesis
Asparagine
Site-Directed Mutagenesis
Oligonucleotides
Endoplasmic Reticulum
Carrier Proteins
Carbohydrates
Peptides
vesicular stomatitis virus G protein

ASJC Scopus subject areas

  • Biochemistry

Cite this

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AB - 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.

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