Figure 8. Residues contributing to the specificity of α5NC1 vs. α3NC1 epitopes.

To differentiate residues that control specificity of α5 epitopes, both of the pathogenic E_A and E_B regions of α3 and α5 chains were aligned and contrasted in terms of identity, hydrophobicity, and isoelectric points (pI). Residues 1, 5, 8, 11, and 15 determine antibodies specificity given low degree of conservation and unique properties (left panel, marked with *). Molecular modeling predicts that spatial organization of the epitopes are similar in context of the hexamer, however, combination of variable residues constitutes unique targets for GP antibodies (right panels).