Recognition requirements for high-entropy residues contribute to strain specificity of 2C06 and 2C09
(A) While neutralization breadth generally correlates with epitope entropy, antibodies directed to the fusion-peptide sites of vulnerability have similar epitope entropy. Neutralization breadth represents the percentage of the 208-strain panel neutralized with IC(B) Analyses of sequence entropy and contact surface areas of residues in strain-specific and broadly neutralizing fusion-peptide-directed antibodies. Epitope residues with normalized entropy above 0.4 are listed, as well as residue S241, which has low entropy but with low frequency as serine among HIV-1 isolates. The contact atoms and areas for VRC34.01 were calculated from PDB: 5i8h (VRC34.01 also binds AMC011 Env, which has valine85). Entropy values were calculated with Shannon Entropy-One ((C) H85, with high Shannon entropy of 0.733 and 2.5% frequency, has tight interactions with antibody heavy- and light-chain residues in both structures of the 2C06 complex (2C09 has nearly identical interactions, see See also KEY RESOURCES TABLE