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 × 106 daltons of protein in the poliovirus particle, indicates that it contains 60 such structural units and that its triangulation number = 1.
AndererF. A.,
RestleH.1964; Untersuchungen über ein attenuiertes Poliomyelitis-Virus Typ 11, Reindarstellung und physikalisch-chemische Eigenschaften des Virus. Zeitschrift für naturforschung 19b:1026–1031
BurnessA. T. H.,
ClothierF. W.1970; Particle weight and other biophysical properties of encephalomyocarditis virus. Journal of General Virology 6:381–394
BurrellC. J. J.,
MartinE. M.,
CooperP. D.1970; Posttranslational cleavage of virus polypeptides in arbovirus-infected cells. Journal of General Virology 6:319–323
CooperP. D.,
GeisslerE.,
ScottiP. D.,
TannockG. A.1971; Further characterisation of the genetic map of poliovirus temperature-sensitive mutants. In Strategy of the Viral Genome. (Ciba Foundation Symposium) pp. 75–100 Edited by
W.G. E.
Wolstenholme and Maeve O’Connor, London: Churchill Livingstone;
DunkerA. K.,
RueckertR. R.1971; Fragments generated by pH dissociation of ME-virus and their relation to the structure of the virion. Journal of Molecular Biology 58:217–235
LaverW. G.1969; Peptide mapping of viral proteins. In Fundamental techniques in virology pp 371–378 Edited by
HabelK.,
SalzmanN. P.
New York: Academic Press;
LevintowL.,
DarnellJ. E.1960; A simplified procedure for purification of large amounts of poliovirus: characterization and amino acid analysis of type 1 poliovirus. Journal of Biological Chemistry 235:70–73
MaizelJ. V.,
SummersD. F.1968; Evidence for differences in size and composition of the poliovirus-specific polypeptides in infected HeLa cells. Virology 36:48–54
RueckertR. R.,
DunkerA. K.,
StoltzfusC. M.1969; The structure of Mouse-Elberfeld virus: a model. Proceedings of the National Academy of Sciences of the United States of America 62:912–919
SchafferF. L.,
SchwerdtC. E.1965; Chemistry of the RNA viruses. In Viral and Rickettsial Infections of Man 4th Edition, pp 94–144 Edited by
HorsfallF. L.,
TammI.
Pennsylvania: Lippincott;
ScharffM. D.,
MaizelJ. V.,
LevintowI.1964; Physical and immunological properties of a soluble precursor of the poliovirus capsid. Proceedings of the National Academy of Sciences of the United States of America 51:329–337
SchwerdtC. E.1957; Physical and chemical characteristics of purified poliomyelitis virus. In Cellular Biology, Nucleic Acids and Viruses pp 159–166 New York: Academy of Sciences;
SchwerdtC. E.,
SchafferF. L.1955; Some physical and chemical properties of purified poliomyelitis virus preparations. Annals of the New York Academy of Sciences 61:740–753
SteinerD. F.,
ClarkJ. L.,
NolanC.,
RubensteinA. H.,
MargoliashE.,
AtenB.,
OyerP. E.1969; Proinsulin and the biosynthesis of insulin. Recent Progress in Hormone Research 25:207–282
TannockG. A.,
GibbsA. J.,
CooperP. D.1970; A reexamination of the molecular weight of poliovirus RNA. Biochemical and Biophysical Research Communications 38:298–304
WatanabeY.,
WatanabeK.,
KatagiriS.,
HinumaY.1965; Virus-specified proteins produced in HeLa cells infected with poliovirus: characterisation of subunit-like protein. Journal of Biochemistry 57:733–741