9CPP
Crystal structure of SARS-CoV-2 receptor binding domain in complex with antibodies M22-17 and CC12.3
Summary for 9CPP
| Entry DOI | 10.2210/pdb9cpp/pdb |
| Descriptor | Spike protein S1, CC12.3 Fab heavy chain, CC12.3 Fab light chain, ... (7 entities in total) |
| Functional Keywords | covid-19, sars-cov-2, receptor binding domain, antibody, immune system, viral protein-immune system complex, viral protein/immune system |
| Biological source | Severe acute respiratory syndrome coronavirus 2 More |
| Total number of polymer chains | 5 |
| Total formula weight | 118603.09 |
| Authors | Feng, Z.,Wilson, I.A. (deposition date: 2024-07-18, release date: 2025-06-25, Last modification date: 2025-08-06) |
| Primary citation | Nair, U.,Feng, Z.,Akauliya, M.,Esposito, A.G.,Crain, C.R.,Lamperti, E.D.,Prum, T.,Warner, J.E.,Madungwe, L.,Dale, G.A.,Boucau, J.,Gaiha, G.D.,Yuan, M.,Wilson, I.A.,Batista, F.D. In vivo antibody diversification targeting a conserved coronavirus epitope. J.Exp.Med., 222:-, 2025 Cited by PubMed Abstract: To explore the use of human B cell receptor (BCR) knock-in mice for broadening antibody responses, we diversified CR3022, a monoclonal antibody (mAb) originally identified in a 2003 severe acute respiratory syndrome coronavirus (SARS-CoV) convalescent patient. This mAb targets a conserved epitope on the coronavirus receptor-binding domain (RBD). We took advantage of high- and low-affinity CR3022 BCR knock-in mice and immunized them with SARS-CoV-2 Wuhan RBD trimers to expand the breadth of these antibodies toward this virus. The resulting antibodies retained the ability to neutralize SARS-CoV and exhibited enhanced affinity and neutralization against the SARS-CoV-2 WA1/2020 strain, as well as the Delta (B.1.617.2) and Omicron KP.3 variants. They also showed broadened reactivity to two bat coronaviruses: WIV1 and, to a lesser potency, BtKY72. Structural analysis revealed key mutations that enhanced binding and neutralization, highlighting the importance of epitope accessibility and variant-specific conformations in antibody diversification. These findings demonstrate that human BCR-expressing mouse models can generate effective antibodies with broad neutralizing activity against viral epitopes. PubMed: 40674170DOI: 10.1084/jem.20241563 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.19 Å) |
Structure validation
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