7BWJ
crystal structure of SARS-CoV-2 antibody with RBD
Summary for 7BWJ
Entry DOI | 10.2210/pdb7bwj/pdb |
Descriptor | Spike protein S1, antibody light chain, antibody heavy chain, ... (4 entities in total) |
Functional Keywords | spike, receptor binding domain, antibody, viral protein |
Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) More |
Total number of polymer chains | 3 |
Total formula weight | 71631.00 |
Authors | |
Primary citation | Ju, B.,Zhang, Q.,Ge, J.,Wang, R.,Sun, J.,Ge, X.,Yu, J.,Shan, S.,Zhou, B.,Song, S.,Tang, X.,Yu, J.,Lan, J.,Yuan, J.,Wang, H.,Zhao, J.,Zhang, S.,Wang, Y.,Shi, X.,Liu, L.,Zhao, J.,Wang, X.,Zhang, Z.,Zhang, L. Human neutralizing antibodies elicited by SARS-CoV-2 infection. Nature, 584:115-119, 2020 Cited by PubMed Abstract: The coronavirus disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) presents a global health emergency that is in urgent need of intervention. The entry of SARS-CoV-2 into its target cells depends on binding between the receptor-binding domain (RBD) of the viral spike protein and its cellular receptor, angiotensin-converting enzyme 2 (ACE2). Here we report the isolation and characterization of 206 RBD-specific monoclonal antibodies derived from single B cells from 8 individuals infected with SARS-CoV-2. We identified antibodies that potently neutralize SARS-CoV-2; this activity correlates with competition with ACE2 for binding to RBD. Unexpectedly, the anti-SARS-CoV-2 antibodies and the infected plasma did not cross-react with the RBDs of SARS-CoV or Middle East respiratory syndrome-related coronavirus (MERS-CoV), although there was substantial plasma cross-reactivity to their trimeric spike proteins. Analysis of the crystal structure of RBD-bound antibody revealed that steric hindrance inhibits viral engagement with ACE2, thereby blocking viral entry. These findings suggest that anti-RBD antibodies are largely viral-species-specific inhibitors. The antibodies identified here may be candidates for development of clinical interventions against SARS-CoV-2. PubMed: 32454513DOI: 10.1038/s41586-020-2380-z PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.85 Å) |
Structure validation
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