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. Author manuscript; available in PMC: 2015 Jul 31.
Published in final edited form as: Cell. 2014 Jul 24;158(3):481–491. doi: 10.1016/j.cell.2014.06.022

Figure 6. Evolutionary mutations in the Loop D and antibody facilitate interactions between gp120 and CH103 lineage antibodies.

Figure 6

(A) Model of CH505 T/F gp120 in complex with UCA of CH103. (B) Model of loop D mutant M7E275K/N279D/V281S gp120 in complex with mature CH103. The gp120 is shown in semi-transparent electrostatic potential surface with red for negative charge and blue for positive charge. The heavy and light chains of the CH103 bnAb are shown in green and orange, respectively. All critical mutations in loop D and CDR L2 are highlighted in sticks and colored in cyan for residues (279 and 281) in loop D, orange for conserved CDR L2 Lys53, and blue for mutated CDR L2 residues 50–52. (C) Calculated binding energy change (ΔΔG) when specified residues were reverted back to the T/F or germline sequences for gp120 and CH103 light chain, respectively. All revertants (except the non-interfacial loop D Lys275) resulted in unfavorable ΔΔG changes (indicated in red in panels a and b) suggesting that the evolution of both gp120 loop D and CDR L2 of CH103 facilitated the interaction between HIV-1 gp120 and mature CH103 antibodies.