EMD-26256

Single-particle
4.8 Å
EMD-26256 Deposition: 17/02/2022
Map released: 30/03/2022
Last modified: 16/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

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-particle
4.8 Å
EMD-26256 Deposition: 17/02/2022
Map released: 30/03/2022
Last modified: 16/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
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
Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529.
PUBMED: 35324257
DOI: doi:10.1126/science.abn8897
ISSN: 1095-9203
ASTM: SCIEAS
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.