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

The effect of zinc ions on the post-translational cleavage of mengovirus polypeptides has been examined. The cleavage of the "A" precursor, which gives rise to the capsid proteins, was the most sensitive at concentrations of zinc chloride from 0.1 to 1.0 mM. Beta-mercaptoethanol and dithiothreitol antagonized the zinc-promoted inhibtion of clevage. Our results indicate that zinc ions interfere with the proper folding of the nascent polypeptide precursor rather than inhibit the proteases responsible for the cleavages. Thus, proper folding of mengovirus polypeptide "A" appears to be necessary for subsequent processing by proteases.