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7TB8

Cryo-EM structure of SARS-CoV-2 spike in complex with antibodies B1-182.1 and A19-61.1

Summary for 7TB8
Entry DOI10.2210/pdb7tb8/pdb
Related7TBF
EMDB information25794
DescriptorSpike 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 Keywordssars-cov-2, spike, antibody, viral protein, viral protein-immune system complex, viral protein/immune system
Biological sourceSevere acute respiratory syndrome coronavirus 2
More
Total number of polymer chains11
Total formula weight508037.10
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 citationZhou, 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: 35324257
DOI: 10.1126/science.abn8897
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.83 Å)
Structure validation

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