The Genome-linked Protein of Picornaviruses. VIII. Complete Amino Acid Sequence of Poliovirus VPg and Carboxy-terminal Analysis of its Precursor, P3-9
- 1 February 1983
- journal article
- research article
- Published by Microbiology Society in Journal of General Virology
- Vol. 64 (2) , 349-355
- https://doi.org/10.1099/0022-1317-64-2-349
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.This publication has 20 references indexed in Scilit:
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