Extended Data Fig. 9: Details for cryo-EM structures of D48 in complex with gB.
From: Prefusion structure, evasion and neutralization of HSV-1 glycoprotein B
a,b, Expanded views of the interaction between D48 and postfusion gB amino acids (a) and glycans (b). c, Visualization of the clash between the D48-enforced conformation of glycan 141 and the prefusion-specific orientation of the helical residues 458-473. d, Highlighting features of the putative fusion-intermediate structure captured by D48 in complex with DS-stabilized gB, including formation of the DIII helical bundle and rearrangement of DV. The arrows indicate the direction of conformational change for DIII and DV from apo prefusion gB. e, Comparison of gB-Ecto.516 P.531E.DS domains DII, DIII and D1V-DV from the aligned prefusion apo (grey) and D48 complex (coloured) structures. Trimeric DIII is shown to emphasize the different conformations of the two structures. Notably, a majority of DV has become disordered in the in the D48 complex.
