Isoelectric Focusing Studies of Mengo Virus Variants, their Protein Structure Units and Constituent Polypeptides Free

Abstract

SUMMARY

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 -ethylene glycol. An examination of -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.

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/content/journal/jgv/10.1099/0022-1317-35-3-425
1977-06-01
2024-03-29
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References

  1. Chlumecka V., D’obrenan P., Colter J. S. 1973; Electrophoretic studies of three variants of Mengo encephalomyelitis virus. Canadian Journal of Biochemistry 51:1521–1526
    [Google Scholar]
  2. Ellem K. A. O., Colter J. S. 1961; The isolation of three variants of Mengo virus differing in plaque morphology and hemagglutinating characteristics. Virology 15:340–347
    [Google Scholar]
  3. Jones R. E., Hemmings W. A., Faulk W. P. 1971; Ethylene glycol as a stabilizing agent in electrofocusing. Immunochemistry 8:299–301
    [Google Scholar]
  4. Korant B. D., Lonberg-holm K., Yin F. H., Noble-Harvey J. 1975; Fractionation of biologically active and inactive populations of human rhinovirus type 2. Virology 63:384–394
    [Google Scholar]
  5. Mak T. W., Colter J. S., Scraba D. G. 1974; Structure of the Mengo virion. II. Physicochemical and electron microscopic analysis of degraded virus. Virology 57:543–553
    [Google Scholar]
  6. Mak T. W., O’callaghan D. J., Colter J. 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
    [Google Scholar]
  7. Mak T. W., O’callaghan D. J., Kay C. M., Colter J. S. 1971; Studies of the protein subunit of pHinactivated Mengo virus variants. II. Physicochemical properties. Virology 3:579–587
    [Google Scholar]
  8. Mandel B. 1971; Characterization of type 1 poliovirus by electrophoretic analysis. Virology 44:554–568
    [Google Scholar]
  9. O’callaghan D. J., Mak T. W., colter J. S. 1970; Studies of the protein subunit of pH-inactivated Mengo virus variants. 1. Polypeptide composition. Virology 42:229–233
    [Google Scholar]
  10. Scraba D. G., Hostvedt P., Colter J. S. 1969; Physical and chemical studies of Mengo virus variants. II.Chromatographic behavior and chemical composition. Canadian Journal of Biochemistry 47:165–171
    [Google Scholar]
  11. Scraba D. F., Hostvedt P., Colter J. 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
    [Google Scholar]
  12. Sever J. L. 1962; Application of a microtechnique to viral serological investigations. Journal of Immunology 88:320–329
    [Google Scholar]
  13. Weber K., Kates D. J. 1971; Reversible denaturation of enzymes by sodium dodecyl sulfate. Journal of Biological Chemistry 246:4504–4509
    [Google Scholar]
  14. Weber K., Osborn M. 1969; The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. Journal of Biological Chemistry 244:4406–4412
    [Google Scholar]
  15. Ziola B. R., Scraba D. O. 1974; Structure of the Mengo virion. I. Polypeptide and ribonucleate components of the virus particle. Virology 57:531–542
    [Google Scholar]
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