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. 1986 Aug;59(2):486–489. doi: 10.1128/jvi.59.2.486-489.1986

Amino-terminal mutation of the vesicular stomatitis virus glycoprotein does not affect its fusion activity.

C Woodgett, J K Rose
PMCID: PMC253100  PMID: 3016308

Abstract

Earlier studies demonstrated that synthetic peptides corresponding to the amino terminus of the vesicular stomatitis virus glycoprotein (G protein) have a pH-dependent hemolytic activity that is thought to be related to the fusion activity of G protein (R. Schlegel and M. Wade, J. Biol. Chem. 259: 4691-4694, 1984; R. Schlegel and M. Wade, J. Virol. 53: 319-323, 1985). A single amino acid change (lysine to glutamic acid at the amino terminus) abolishes the hemolytic activity of the peptide. Here we used oligonucleotide-directed mutagenesis to create a DNA encoding G protein with this same amino acid change at its amino terminus. The mutant protein encoded by this gene was expressed transiently in a monkey fibroblast cell line (COS) and was found to have a pH-dependent fusion activity indistinguishable from wild-type G protein. This result indicates that the hemolytic activity of the synthetic peptides was not related to the fusion activity of the G protein.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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