Fig. 3: Structural basis for VRC34.01-Combo1’s recognition of diverse FP. | Nature Communications

Fig. 3: Structural basis for VRC34.01-Combo1’s recognition of diverse FP.

From: Antibody-directed evolution reveals a mechanism for enhanced neutralization at the HIV-1 fusion peptide site

Fig. 3: Structural basis for VRC34.01-Combo1’s recognition of diverse FP.The alternative text for this image may have been generated using AI.

A Crystal structure of VRC34.01-Combo1 Fab in complex with fusion peptide variant FP8_v1. B CryoEM structure of BG505 DS-SOSIP HIV trimer in complex with the VRC34.01_Combo1 Fab. C, D Details of interactions between VRC34.01-Combo1 (cyan/orange/magenta) bound to peptide FP8v1 (AVGIGAVF) that provided improved neutralization breadth compared to parental VRC34.01 (green/yellow/violet). E Representative electron density around critical residues W50HC, F58HC, Y94LC, V513FP, G514FP, and I515FP.

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