Key result
Foot-and-mouth disease virus 3C protease cleaves translation initiation factor eIF4AI between residues E143 and V144, but not the closely related eIF4AII, leading to its expected inactivation.
The study identifies the specific cleavage site of eIF4AI by FMDV 3C protease, providing insight into the mechanism of viral interference with host translation.
Elucidates FMDV 3Cpro isoform specificity; leaves open its role in pathogenesis and antiviral targeting.
The translation initiation factor eIF4A is cleaved within mammalian cells infected by foot-and-mouth disease virus (FMDV). The FMDV 3C protease cleaves eIF4AI (between residues E143 and V144), but not the closely related eIF4AII. Modification of eIF4AI, to produce a sequence identical to eIF4AII around the cleavage site, blocked proteolysis. Alignment of mammalian eIF4AI onto the three-dimensional structure of yeast eIF4A located the scissile bond within an exposed, flexible portion of the molecule. The N- and C-terminal cleavage products of eIF4AI generated by FMDV 3C dissociate. Cleavage of eIF4AI by FMDV 3C is thus expected to inactivate it.
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Li et al. (2001) studied Foot-and-mouth disease virus (FMDV) infection. FMDV 3C protease vs. eIF4AII was evaluated on Cleavage of eIF4A. Foot-and-mouth disease virus 3C protease cleaves translation initiation factor eIF4AI between residues E143 and V144, but not the closely related eIF4AII, leading to its expected inactivation.
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