Virion polypeptide heterogeneity among virulent and avirulent strains of eastern equine encephalitis (EEE) virus. 
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 X 10(3) for (E-1), 51-54 X 10(3) for (E-2) and 35-38 X 10(3) 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-/ 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 reported in vitro characteristics (antigenic subtypes, HTP elution profiles) nor with the in vivo virulence markers.