7TB8
Cryo-EM structure of SARS-CoV-2 spike in complex with antibodies B1-182.1 and A19-61.1
Summary for 7TB8
Entry DOI | 10.2210/pdb7tb8/pdb |
Related | 7TBF |
EMDB information | 25794 |
Descriptor | Spike glycoprotein, The heavy chain of SARS-CoV-2 antibody A19-61.1, The light chain of SARS-COV-2 antibody A19-61.1, ... (8 entities in total) |
Functional Keywords | sars-cov-2, spike, antibody, viral protein, viral protein-immune system complex, viral protein/immune system |
Biological source | Severe acute respiratory syndrome coronavirus 2 More |
Total number of polymer chains | 11 |
Total formula weight | 508037.10 |
Authors | Zhou, T.,Tsybovsky, T.,Kwong, P.D. (deposition date: 2021-12-21, release date: 2022-03-30, Last modification date: 2024-11-13) |
Primary citation | Zhou, T.,Wang, L.,Misasi, J.,Pegu, A.,Zhang, Y.,Harris, D.R.,Olia, A.S.,Talana, C.A.,Yang, E.S.,Chen, M.,Choe, M.,Shi, W.,Teng, I.T.,Creanga, A.,Jenkins, C.,Leung, K.,Liu, T.,Stancofski, E.D.,Stephens, T.,Zhang, B.,Tsybovsky, Y.,Graham, B.S.,Mascola, J.R.,Sullivan, N.J.,Kwong, P.D. Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529. Science, 376:eabn8897-eabn8897, 2022 Cited by PubMed Abstract: The rapid spread of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) B.1.1.529 (Omicron) variant and its resistance to neutralization by vaccinee and convalescent sera are driving a search for monoclonal antibodies with potent neutralization. To provide insight into effective neutralization, we determined cryo-electron microscopy structures and evaluated receptor binding domain (RBD) antibodies for their ability to bind and neutralize B.1.1.529. Mutations altered 16% of the B.1.1.529 RBD surface, clustered on an RBD ridge overlapping the angiotensin-converting enzyme 2 (ACE2)-binding surface and reduced binding of most antibodies. Substantial inhibitory activity was retained by select monoclonal antibodies-including A23-58.1, B1-182.1, COV2-2196, S2E12, A19-46.1, S309, and LY-CoV1404-that accommodated these changes and neutralized B.1.1.529. We identified combinations of antibodies with synergistic neutralization. The analysis revealed structural mechanisms for maintenance of potent neutralization against emerging variants. PubMed: 35324257DOI: 10.1126/science.abn8897 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.83 Å) |
Structure validation
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