Multiple proteases in foot-and-mouth disease virus replication

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Abstract
Translation of foot-and-mouth disease virus RNA in a rabbit reticulocyte lysate for short time intervals resulted in the production of the peptides P20a, P16 and P88. If further translation was prevented, the structural protein precursor P88 was not cleaved, even after prolonged incubation. Evidently, the mechanism of the cleavage between P20a-P16 and P88 and of that between P88 and P52 (P2) differs from the mechanism of the secondary cleavages which produce the structural proteins. Treatment of foot-and-mouth disease virus-infected hamster kidney BHK-21 cells with the protease inhibitor D-valyl phenylalanyl lysyl chloromethyl ketone prevented the in vivo cleavage between P20a-P16 and P88, but had no effect on any of the other cleavage events. Apparently, the cleavage of the foot-and-mouth disease virus polyprotein utilizes 2 different host proteases.