9CFE
Cryo-EM Local Refinement of Antibody 19-77 in complex with prefusion SARS-CoV-2 Spike glycoprotein RBD
Summary for 9CFE
| Entry DOI | 10.2210/pdb9cfe/pdb |
| EMDB information | 45543 |
| Descriptor | heavy chain, light chain, Spike protein S1 (3 entities in total) |
| Functional Keywords | neutralizing antibody, viral fusion protein, sars-cov-2, viral protein-immune system complex, viral protein, viral protein/immune system |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 3 |
| Total formula weight | 46144.59 |
| Authors | Casner, R.G.,Shapiro, L. (deposition date: 2024-06-27, release date: 2025-07-02, Last modification date: 2025-10-01) |
| Primary citation | Wang, Q.,Guo, Y.,Casner, R.G.,Yu, J.,Nair, M.S.,Ho, J.,Reddem, E.R.,Mellis, I.A.,Wu, M.,Tzang, C.C.,Hong, H.,Huang, Y.,Shapiro, L.,Liu, L.,Ho, D.D. Optimizing a human monoclonal antibody for better neutralization of SARS-CoV-2. Nat Commun, 16:6195-6195, 2025 Cited by PubMed Abstract: SARS-CoV-2 has largely evolved to resist antibody pressure, with each successive viral variant becoming more and more resistant to serum antibodies in the population. This evolution renders all previously authorized anti-spike therapeutic monoclonal antibodies inactive, and it threatens the remaining pipelines against COVID-19. We report herein the isolation of a human monoclonal antibody with a broad but incomplete SARS-CoV-2 neutralization profile, but structural analyses and mutational scanning lead to the engineering of variants that result in greater antibody flexibility while binding to the viral spike. Three such optimized monoclonal antibodies neutralize all SARS-CoV-2 strains tested with much improved potency and breadth, including against subvariants XEC and LP.8.1. The findings of this study not only present antibody candidates for clinical development against COVID-19, but also introduce an engineering approach to improve antibody activity via increasing conformational flexibility. PubMed: 40615407DOI: 10.1038/s41467-025-61472-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.03 Å) |
Structure validation
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