Summary
Comparative analysis of structural virion polypeptides of 24 selected EEE virus strains, representing North and South American types, was performed by one-dimensional discontinuous sodium dodecyl sulfate (SDS)-polyacrylamide-gel electrophoresis (PAGE). The structural proteins of different EEE virus isolates, resolved by this method, exhibited mol.wts. values in the range of 57–60 × 103 for (E-1), 51–54 × 103 for (E-2) and 35–38 × 103 daltons for the core (NP) nucleocapsid. The exception was the South American human lethal virus, TRVL-89287 strain, which was shown to possess only a single envelope glycoprotein. The high molecular weight envelope (E-1) glycoprotein species was absent or co-migrated adjacent to the smaller envelope (E-2) glycoprotein. Results indicated similarities in the core (NP) proteins, however greater variability in the envelope (E-1 and/or E-2) glycoproteins. Based on these variations seven distinct profiles could be observed among the EEE virus strain studied. The classification based on the patterns of structural polypeptides obtained by SDS-PAGE of these strains does not correlate well with any other previously reportedin vitro characteristics (antigenic subtypes, HTP elution profiles) nor with thein vivo virulence markers.
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Walder, R., Rosato, R.R. & Eddy, G.A. Virion polypeptide heterogeneity among virulent and avirulent strains of eastern equine encephalitis (EEE) virus. Archives of Virology 68, 229–237 (1981). https://doi.org/10.1007/BF01314576
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DOI: https://doi.org/10.1007/BF01314576