Relationship between synthesis and cleavage of poliovirus-specific proteins.

AUTOR(ES)

Thomas, A A

RESUMO

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.

Documentos Relacionados

• Cleavage of Poliovirus-Specific Polypeptide Aggregates
• Inhibition of Cleavage of Large Poliovirus-Specific Precursor Proteins in Infected HeLa Cells by Inhibitors of Proteolytic Enzymes
• Poliovirus-specific primer-dependent RNA polymerase able to copy poly(A).
• Poliovirus-specific immunoglobulin A in persons vaccinated with inactivated poliovirus vaccine in The Netherlands.
• Characterization of poliovirus-specific T lymphocytes in the peripheral blood of Sabin-vaccinated humans.