Fig. 1: The point mutation H527P constrains VZV gB in a prefusion conformation. | Nature Communications

Fig. 1: The point mutation H527P constrains VZV gB in a prefusion conformation.

From: Targeted mutagenesis of the herpesvirus fusogen central helix captures transition states

Fig. 1: The point mutation H527P constrains VZV gB in a prefusion conformation.The alternative text for this image may have been generated using AI.

a A diagram of the linear structure for VZV gB highlighting the location of the DIII central helix. The signal sequence is depicted by the crossed white box. Colored regions (residues 115–736) correspond to domains in the cryo-EM structure; DI (cyan), DII (green), DIII (yellow), DIV (orange), DV (red) and linker regions (hot pink). Amino acids 526EHV528 (bold) were targeted for mutagenesis. b and c Trimer and monomer models for VZV gB prefusion (b) by SWISS Model20 and postfusion (c) from the 2.8 Å cryo-EM structure3. The inset shows the 526EHV528 site in the DIII central helix. d Single plane views of representative tomographic reconstructions (see Supplementary Table 1) from cryo-ET of EVs produced by BHK-21 cells transfected with gB[H527P] or WT gB expression vectors. Upper and lower panels are different planes from the same tomogram to show side and top views of gB[H527P] or WT gB expressed on EVs. Boxes with dashed lines are magnified areas shown in the insets. Scale bars shown are for each panel and inset.

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