7TC9

Locally refined region of SARS-CoV-2 spike in complex with antibody A19-46.1

Summary for 7TC9

• Entry DOI: 10.2210/pdb7tc9/pdb
• EMDB information: 25806
• Descriptor: Spike protein S1, Heavy chain of antibody A19-46.1, Light chain of antibody A19-46.1, ... (4 entities in total)
• Functional Keywords: sars-cov-2, omicron, spike, antibody, viral protein, viral protein-immune system complex, viral protein/immune system
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 3
• Total formula weight: 70034.46

Authors

Zhou, T.,Kwong, P.D. (deposition date: 2021-12-23, release date: 2022-03-30, Last modification date: 2024-11-20)

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

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

Experimental method

ELECTRON MICROSCOPY (5.08 Å)