Abstract
VPg, the genome-linked protein of poliovirus, and its putative precursor P3-9, were radiolabeled and subjected to carboxypeptidase-A digestion. The release of amino acids was followed by identification and quantification on an amino acid analyzer. Both proteins were found to be co-terminal with a sequence of -valyl-glutamine-COOH, an observation that provides further evidence that host cell trimming of virus-specific peptides does not play a role in poliovirus protein processing. Radiolabeled VPg was subjected to automated Edman degradation. The combined results complete the structural analysis of VPg, a polypeptide 22 amino acids in length with a MW of 2354. Only 1 form of VPg was found linked to virion RNA and it originates by a cleavage at glutaminyl-glycine pairs at both termini. The observation is consistent with other cleavages found in the virus processing scheme.

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