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J Gen Virol 64 (1983), 349-355; DOI 10.1099/0022-1317-64-2-349
© 1983 Society for General Microbiology
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The Genome-linked Protein of Picornaviruses. VIII. Complete Amino Acid Sequence of Poliovirus VPg and Carboxy-terminal Analysis of its Precursor, P3-9

Cheryl J. Adler1, Marshall Elzinga2 and Eckard Wimmer1

1 Department of Microbiology, School of Medicine, State University of New York at Stony Brook, Stony Brook, New York 11794
and2 Department of Biology, Brookhaven National Laboratory, Upton, New York 11973, U.S.A.

VPg, the genome-linked protein of poliovirus, and its putative precursor P3-9, were radiolabelled and subjected to carboxypeptidase-A digestion. The release of amino acids was followed by identification and quantification on an amino acid analyser. 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. Radiolabelled 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 molecular weight of 2354. Only one form of VPg has been 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.

Keywords: poliovirus VPg/precursor P3-9, carboxypeptidase, Edman degradation

Received 28 March 1982; accepted 17 August 1982.




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Copyright © 1983 by the Society for General Microbiology.