Fig. 7

Cryo-EM reconstruction of 7B3-RBD complex and structure superposition. a (Left)The overall structure of 7B3 Fab in complex with SARS-CoV-2 S-6P trimer. One Fab (light chain in teal, heavy chain in pink) bounded RBD is in the “down” position, and the Fab bound spike protomer colored in beige and the other two in gray, and the local refinement region is boxed with black dash. (Right) Side view of 14B1 bound to RBD model after local refinement, and the N343 linked glycan is shown as red sphere. b Top view of 7B3 bound RBD. The CDR loops are labeled, RBD is shown as beige surface, and hACE2 binding sites are colored in light gray. c Interactions between RBD and CDRL3 loop. The residues bound with CDRL3 are shown in green stick. CDRL3 are in teal and the residues bound with RBD are shown in gray stick models. The yellow dashes represent hydrogen bonds and salt bridges. Residues 483–490 (VEGFNCYF) are colored in coral. d Stereo pairs showing interactions between heavy chain and RBD. The color scheme is similar to (c). e Structure superposition of 14B1-RBD and 7B3-RBD. (Left) 14B1 (slate blue ribbon model) and 7B3 (pink ribbon model) both bind to the top face of RBD. (Right) Top view of the epitopes of 14B1 and 7B3, and the epitopes of two Fabs are partially overlapped. Epitopes unique to the two antibodies are labeled separately. f Mutated residues contacted by 14B1 or 7B3 on SARS-CoV-2 WT RBD in comparison with Omicron variants are shown as spheres. Color scheme is similar to (e)