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.
| Original language | English |
|---|---|
| Pages (from-to) | 309-13 |
| Number of pages | 5 |
| Journal | Journal of Virology |
| Volume | 48 |
| Issue number | 1 |
| Publication status | Published - 1983 |
Keywords
- Endopeptidases
- HeLa Cells
- Peptide Chain Initiation, Translational
- Poliovirus
- Protein Biosynthesis
- Protein Precursors
- RNA, Viral
- Viral Proteins
