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Genetic and Structural Implications of Tryptic Peptide Analysis of Poliovirus Structural Protein

Department of Microbiology, John Curtin School of Medical Research, Australian National University, Canberra, A.C.T., Australia

D. J. Bennett

Department of Genetics, Research School of Biological Sciences, Australian National University, Canberra, A.C.T., Australia

A count of specifically labelled tryptic peptides from purified poliovirus (strain Mahoney) showed that the amino acid sequence comprising its structural protein contains at least 21 and 25 uniquely placed residues of histidine and methionine, respectively. Amino acid analysis after performic acid oxidation showed a content of, respectively, 21 and 27 moles of these residues per 1000 amino acids recovered. Accordingly, poliovirus structural protein must comprise a unique sequence of about 1000 amino acids, representing about 40% of the coding potential of the poliovirus genome. The correspondence of this percentage with the proportion of the poliovirus genetic map occupied by structural protein genes (48%) suggests that the map represents a major part of the genome. A value of about 1000 amino acids, or 100 to 110000 daltons of protein, for the repeating structural unit, coupled with a total content of 6.0 to 6.4 x 10⁶ daltons of protein in the poliovirus particle, indicates that it contains 60 such structural units and that its triangulation number = 1.

Received 22 September 1972; accepted 5 March 1973.