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. 1980 Jun;34(3):598–603. doi: 10.1128/jvi.34.3.598-603.1980

Defective mutant of Sindbis virus with a smaller-molecular-weight form of the E1 glycoprotein.

A Leone, V Colantuoni, G Pontarelli, R Cancedda
PMCID: PMC288747  PMID: 7381993

Abstract

We have isolated from a single plaque a mutant of Sindbis virus characterized by an E1 glycoprotein with higher electrophoretic mobility. This higher mobility is not attributable to a different extent of glycosylation of the protein nor to an altered proteolytic maturation pathway of the polypeptide precursor, but is the result of a deletion occurring during the replication of the viral RNA. The 26S RNA (the messenger for the Sindbis structural proteins) extracted from cells infected with the mutant is about 0.75 x 10(5) daltons smaller than the 26S RNA from the parental strain. As a consequence, in cells infected with the mutant, an E1 glycoprotein is synthesized with a polypeptide chain about 70 amino acids shorter. The biological relevance of this naturally occurring deletion of the viral genome is discussed.

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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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