Virions of three plaque variants (L-, M- and S-) of Mengo virus, which assume a bimodal distribution when subjected to isoelectric focusing in sucrose-stabilized pH gradients containing 0.5% Brij 35, were found to band in a single peak (at pH 8.1 to 8.4) when focused under the same conditions in gradients supplemented with 6 m-ethylene glycol. An examination of m-Mengo virions, isoelectric at pHs 4.7 and 8.4 in sucrose-stabilized gradients, showed that the two populations were indistinguishable on the basis of specific infectivity, polypeptide composition and sedimentation characteristics, but differed in their ability to agglutinate human erythrocytes.
When pH-inactivated virions were subjected to isoelectric focusing, three well defined peaks were produced, one of which was found to correspond to the well characterized 13.4S subunit of Mengo virus, and the other two — on the basis of compositional analysis — to virions that had lost some of their 13.4S structure units. No difference in electrophoretic behaviour was found among the 13.4S subunits isolated from the three Mengo variants — all three were found to be isoelectric at pH 5.85 to 6.00. Analysis, by isoelectric focusing, of the four structural polypeptides (α, β, γ, δ) isolated from L-, M- and S-Mengo failed to reveal any significant differences among the three variants.
ChlumeckaV.,
D’obrenanP.,
ColterJ. S.1973; Electrophoretic studies of three variants of Mengo encephalomyelitis virus. Canadian Journal of Biochemistry 51:1521–1526
EllemK. A. O.,
ColterJ. S.1961; The isolation of three variants of Mengo virus differing in plaque morphology and hemagglutinating characteristics. Virology 15:340–347
KorantB. D.,
Lonberg-holmK.,
YinF. H.,
Noble-HarveyJ.1975; Fractionation of biologically active and inactive populations of human rhinovirus type 2. Virology 63:384–394
MakT. W.,
ColterJ. S.,
ScrabaD. G.1974; Structure of the Mengo virion. II. Physicochemical and electron microscopic analysis of degraded virus. Virology 57:543–553
MakT. W.,
O’callaghanD. J.,
ColterJ. S.1970; Studies of the early events of the replicative cycle of three variants of Mengo encephalomyelitis virus in mouse fibroblast cells. Virology 42:1087–1096
MakT. W.,
O’callaghanD. J.,
KayC. M.,
ColterJ. S.1971; Studies of the protein subunit of pHinactivated Mengo virus variants. II. Physicochemical properties. Virology 3:579–587
O’callaghanD. J.,
MakT. W.,
colterJ. S.1970; Studies of the protein subunit of pH-inactivated Mengo virus variants. 1. Polypeptide composition. Virology 42:229–233
ScrabaD. G.,
HostvedtP.,
ColterJ. S.1969; Physical and chemical studies of Mengo virus variants. II.Chromatographic behavior and chemical composition. Canadian Journal of Biochemistry 47:165–171
ScrabaD. F.,
HostvedtP.,
ColterJ. S.1970; Physical and chemical studies of Mengo virus variants. II.Absorbance-temperature profiles, sedimentation in dextran sulfate gradients, and total/infectious particle ratios. Canadian Journal of Biochemistry 48:412–417
WeberK.,
OsbornM.1969; The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. Journal of Biological Chemistry 244:4406–4412