Abstract
Poliovirus mutant 2A-1, which encodes a defective protease 2A, fails to inhibit translation of capped mRNAs selectively. Despite the failure of 2A-1 to inactivate cap-dependent translation, a reduction in the overall rate of protein synthesis, both virus and cells-specified, does occur after 2A-1 infection. This global reduction in protein synthesis is temporally correlated with an increase in [Na +] i and a decrease in [K +] i The extensive global shutoff of protein synthesis is not observed in 2A-1 infected cellss incubated in low NaCl medium or medium containing an elevated concentration of KCl which compensate for the virally-induced alterations in intracellsular monovalent cation concentrations. Furthermore, 2A-1-specified protein synthesis is only partly resistant to hypertonic NaCl media which increase [Na +] i, in contrast to protein synthesis specified by wild-type poliovirus. These results suggest that shutoff of host and viral protein synthesis during infection by poliovirus mutant 2A-1 is a consequence of the virus-induced changes in intracellsular monovalent cation concentrations.
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