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. 1983 Oct;48(1):309–313. doi: 10.1128/jvi.48.1.309-313.1983

Relationship between synthesis and cleavage of poliovirus-specific proteins.

A A Thomas, H O Voorma, A Boeye
PMCID: PMC255348  PMID: 6310152

Abstract

Poliovirus proteinase was studied in vitro in lysates from poliovirus-infected HeLa cells. Preincubation of these lysates caused (i) a reduction in poliovirus proteinase activity and (ii) a partial dependence on exogenous mRNA for optimal translation. Proteins translated from endogenous poliovirus RNA in preincubated extracts from virus-infected HeLa cells are poorly cleaved. This cleavage deficiency is alleviated by adding fresh poliovirus RNA to the translation system, thus, allowing re-initiation to occur. This suggests that the poliovirus proteinase is highly unstable.

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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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