Abstract
Eukaryotic initiation factor (eIF) 4GI is efficiently cleaved during picornaviral replication. eIF4GI processing has also recently been observed during HIV-1 replication. We have compared the efficiency of eIF4GI proteolysis in rabbit reticulocyte lysates during translation of mRNAs encoding the foot-and-mouth disease virus leader proteinase (L pro) or the HIV-1 proteinase (HIV-1 pro). L pro cleaved 50% eIF4GI within 12 min whereas HIV-1 pro required 4 h; the concentrations were 2 pg/μl (0.1 nM) for L pro and 60 pg/μl (2.66 nM) for HIV-1 pro. HIV-1 pro processing of eIF4GI is therefore not quantitatively analogous to that of L pro, suggesting that the primary function of eIF4GI cleavage in HIV-1 replication may not be protein synthesis inhibition.
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