EMD-26256
Local refinement of cryo-EM structure of the interface of the Omicron RBD in complex with antibodies B-182.1 and A19-46.1
EMD-26256
Single-particle4.8 Å
![EMD-26256](https://www.ebi.ac.uk/emdb/images/entry/EMD-26256/400_26256.gif)
Map released: 30/03/2022
Last modified: 16/10/2024
Sample Organism:
Homo sapiens,
Severe acute respiratory syndrome coronavirus 2
Sample: Ternary complex of SARS-CoV-2 Omicron RBD in complex with antibodies B1-182.1 and A19-46.1
Fitted models: 7u0d (Avg. Q-score: 0.236)
Deposition Authors: Zhou T
,
kwong PD
Sample: Ternary complex of SARS-CoV-2 Omicron RBD in complex with antibodies B1-182.1 and A19-46.1
Fitted models: 7u0d (Avg. Q-score: 0.236)
Deposition Authors: Zhou T
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Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529.
Zhou T
,
Wang L
,
Misasi J
,
Pegu A
,
Zhang Y
,
Harris DR
,
Olia AS
,
Talana CA
,
Yang ES
,
Chen M
,
Choe M
,
Shi W
,
Teng IT
,
Creanga A
,
Jenkins C
,
Leung K
,
Liu T
,
Stancofski ED,
Stephens T,
Zhang B
,
Tsybovsky Y
,
Graham BS
,
Mascola JR
,
Sullivan NJ
,
Kwong PD
(2022) Science , 376 , eabn8897 - eabn8897
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(2022) Science , 376 , eabn8897 - eabn8897
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.
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.