Fig. 6: Cryo-EM structures of the antibodies WS.HSV-1.24 and D48 in complex with HSV-1 gB reveal mechanisms of gB neutralization. | Nature Microbiology

Fig. 6: Cryo-EM structures of the antibodies WS.HSV-1.24 and D48 in complex with HSV-1 gB reveal mechanisms of gB neutralization.

From: Prefusion structure, evasion and neutralization of HSV-1 glycoprotein B

Fig. 6: Cryo-EM structures of the antibodies WS.HSV-1.24 and D48 in complex with HSV-1 gB reveal mechanisms of gB neutralization.

a, Structure (left) and expanded view (right) of the interaction of prefusion-specific Fab WS.HSV-1.24 with HSV-1 gB-Ecto.H516P.L531E. Select features of WS.HSV-1.24 contact residues (labelled red throughout) are highlighted below. Heavy- and light-chain WS.HSV-1.24 and their specific residue labels are shown in purple and grey, respectively. DI and DII are shown in blue and green, respectively. b, WS.HSV-1.24 recognition of refolding, solvent-exposed, non-glycan-shielded residues. The underlined residues correspond to those in the bottom panel of a. c, Structures of Fab D48 in complex with three different gB-Ecto variants (top) and a matrix of the molecular phenotypes (bottom). Light- and heavy-chain D48 are shown in yellow and pink, respectively.

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