Processing of mengovirus precursor polypeptides in the presence of zinc ions and sulfhydryl compounds

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Abstract
The effect of Zn2+ on the post-translational cleavage of mengovirus polypeptides was examined. The cleavage of the A precursor, which gives rise to the capsid proteins, was most sensitive at concentrations of ZnCl2 from 0.1-1.0 mM. .beta.-Mercaptoethanol and dithiothreitol antagonized the Zn-promoted inhibition of cleavage. Zn2+ may interfere with the proper folding of the nascent polypeptide precursor rather than inhibit the proteases responsible for the cleavages. Proper folding of mengovirus polypeptide A appears to be necessary for subsequent processing by proteases.