7VN9

Crystal structure of human coronavirus 229E spike protein receptor-binding domain in complex with C04 Fab

Summary for 7VN9

• Entry DOI: 10.2210/pdb7vn9/pdb
• Descriptor: C04 Fab heavy chain, C04 Fab light chain, Spike glycoprotein S1, ... (6 entities in total)
• Functional Keywords: neutralizing antibody, human coronavirus 229e, c04 fab., immune system, viral protein-immune system complex, viral protein/immune system
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 6
• Total formula weight: 129503.33

Authors

Xiang, J.C.,Yang, B. (deposition date: 2021-10-10, release date: 2022-10-26, Last modification date: 2024-10-16)

Primary citation

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.
Antigenic mapping reveals sites of vulnerability on alpha-HCoV spike protein.
Commun Biol, 5:1179-1179, 2022

PubMed Abstract: Understanding 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 α-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-α-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 α-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.

PubMed: 36333470
DOI: 10.1038/s42003-022-04160-8

Experimental method

X-RAY DIFFRACTION (4.49 Å)