8QH0
Crystal structure of the SARS-CoV-2 RBD with the antibody Cv2.3194
Summary for 8QH0
Entry DOI | 10.2210/pdb8qh0/pdb |
Descriptor | Spike protein S1, Cv2.3194 Heavy chain, IGK@ protein, ... (7 entities in total) |
Functional Keywords | coronavirus neutralizing antibody, viral protein |
Biological source | Severe acute respiratory syndrome coronavirus 2 More |
Total number of polymer chains | 3 |
Total formula weight | 70993.04 |
Authors | Fernandez, I.,Rey, F.A. (deposition date: 2023-09-06, release date: 2024-06-19, Last modification date: 2025-07-02) |
Primary citation | Planchais, C.,Fernandez, I.,Chalopin, B.,Bruel, T.,Rosenbaum, P.,Beretta, M.,Dimitrov, J.D.,Conquet, L.,Donati, F.,Prot, M.,Porrot, F.,Planas, D.,Staropoli, I.,Guivel-Benhassine, F.,Baquero, E.,van der Werf, S.,Haouz, A.,Simon-Loriere, E.,Montagutelli, X.,Maillere, B.,Rey, F.A.,Guardado-Calvo, P.,Nozach, H.,Schwartz, O.,Mouquet, H. Broad sarbecovirus neutralization by combined memory B cell antibodies to ancestral SARS-CoV-2. Iscience, 27:110354-110354, 2024 Cited by PubMed Abstract: Antibodies play a pivotal role in protecting from SARS-CoV-2 infection, but their efficacy is challenged by the continuous emergence of viral variants. In this study, we describe two broadly neutralizing antibodies cloned from the memory B cells of a single convalescent individual after infection with ancestral SARS-CoV-2. Cv2.3194, a resilient class 1 anti-RBD antibody, remains active against Omicron sub-variants up to BA.2.86. Cv2.3132, a near pan-Sarbecovirus neutralizer, targets the heptad repeat 2 membrane proximal region. When combined, Cv2.3194 and Cv2.3132 form a complementary SARS-CoV-2 neutralizing antibody cocktail exhibiting a local dose-dependent synergy. Thus, remarkably robust neutralizing memory B cell antibodies elicited in response to ancestral SARS-CoV-2 infection can withstand viral evolution and immune escape. The cooperative effect of such antibody combination may confer a certain level of protection against the latest SARS-CoV-2 variants. PubMed: 39071888DOI: 10.1016/j.isci.2024.110354 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.87 Å) |
Structure validation
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