Structural basis for development of neutralization breadth of vFP antibodies.

<p><b>A</b>. Left. CryoEM map of quaternary complex with antibody vFP1.01, segmented by components at a contour level that allowed visualization of Fv domains of antibodies. Right. Zoom-in of the fusion peptide region showing vFP1.01 bound with its CDR loops color-coded. <b>B</b>. Same as A, but with vFP7.04. <b>C</b>. Fusion peptide recognition by vFP1.01, vFP7.04, vFP16.02 and vFP20.01. <b>D</b>. Surface area buried at Env interface by the heavy and light chains of vFP1.01, vFP7.04, vFP20.01, vFP16.02 and VRC34. <b>E</b>. vFP antibody-bound fusion peptide with electron density from the cryo-EM reconstructions shown as blue mesh. All maps were low pass filtered to 4.5 Å. <b>F</b>. Light chain/heavy chain electron density ratio vs. neutralization breadth. The Pearson’s R correlation coefficient is shown.