7vn9
Crystal structure of human coronavirus 229E spike protein receptor-binding domain in complex with C04 Fab
Structural highlights
Publication Abstract from PubMedUnderstanding the antigenic signatures of all human coronaviruses (HCoVs) Spike (S) proteins is imperative for pan-HCoV epitopes identification and broadly effective vaccine development. To depict the currently elusive antigenic signatures of alpha-HCoVs S proteins, we isolated a panel of antibodies against the HCoV-229E S protein and characterized their epitopes and neutralizing potential. We found that the N-terminal domain of HCoV-229E S protein is antigenically dominant wherein an antigenic supersite is present and appears conserved in HCoV-NL63, which holds potential to serve as a pan-alpha-HCoVs epitope. In the receptor binding domain, a neutralizing epitope is captured in the end distal to the receptor binding site, reminiscent of the locations of the SARS-CoV-2 RBD cryptic epitopes. We also identified a neutralizing antibody that recognizes the connector domain, thus representing the first S2-directed neutralizing antibody against alpha-HCoVs. The unraveled HCoVs S proteins antigenic similarities and variances among genera highlight the challenges faced by pan-HCoV vaccine design while supporting the feasibility of broadly effective vaccine development against a subset of HCoVs. Antigenic mapping reveals sites of vulnerability on alpha-HCoV spike protein.,Xiang J, Su J, Lan Q, Zhao W, Zhou Y, Xu Y, Niu J, Xia S, Qi Q, Sidhu S, Lu L, Miersch S, Yang B Commun Biol. 2022 Nov 4;5(1):1179. doi: 10.1038/s42003-022-04160-8. PMID:36333470[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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