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. Author manuscript; available in PMC: 2009 Oct 1.
Published in final edited form as: Immunol Rev. 2008 Oct;225:212–225. doi: 10.1111/j.1600-065X.2008.00676.x

Fig. 4. Relationship between epitope accessibility and the occupancy requirements for neutralization.

Fig. 4

The accessibility of epitopes recognized by two different mAbs on the mature WNV virion is illustrated using molecular modeling: residues that comprise each determinant are illustrated as solid spheres. E proteins are colored according to their proximity to the 2-, 3-, or 5-fold symmetry axes (blue, green, and yellow, respectively). The number of accessible binding sites for each antibody is indicated on the left, whereas the ‘threshold’ for neutralization is indicated as a red line (modeled in this instance as 30 mAbs based on studies using the mAb E16). To exceed the threshold requirements for neutralization, only a fraction of highly accessible determinants must be simultaneously occupied by antibody (a low occupancy requirement). For cryptic epitopes (fewer accessible sites), a significantly greater percentage of accessible epitopes must be bound to achieve the same number of antibodies docked on the average virion (a high occupancy requirement). Adapted from (112, 139).