The N-terminus of varicella-zoster virus glycoprotein B has a functional role in fusion
Fig 2
Subnanometer resolution cryo-EM structures of Fab fragments from either 93k or SG2 in complex with native, full-length VZV gB purified from VZV infected MeWo cells.
A to C–Subnanometer resolution cryo-EM maps of gB-93k (93k –blue; 7.3Å) and gB-SG2 (SG2 –green; 9.0Å) complexes focused at the gB-Fab fragment interface (A and B), viewed from the side and top (C) and a composite cryo-EM map of the 93k and SG2 Fabs bound to native gB showing the difference in binding angles of the two Fabs. The Fab binding angles were calculated from the central axis of gB (vertical line) and the central axes of the 93k and SG2 Fabs. The gB ectodomain is shown in grey and the CTD show in red; the CTD is depicted at a different threshold to the ectodomain due to the lower resolution for this part of the cryo-EM map. D–A linear map of VZV gB showing the location of the mAb 93k major binding sites (β23 and β30) and the predicted mAb SG2 binding site (β25 and β26) in gB DIV. The gB furin cleavage site is shown. VZV gB domains are colored as follows, DI (cyan), DII (green), DIII (yellow), DIV (orange), DV (red) and linker regions (hot pink).