Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529-Reference-Cited by-同舟云学术

Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529

Published:2022-04-22 Issue:6591 Volume:376 Page:
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Zhou Tongqing¹^ORCID,Wang Lingshu¹^ORCID,Misasi John¹^ORCID,Pegu Amarendra¹^ORCID,Zhang Yi¹^ORCID,Harris Darcy R.¹,Olia Adam S.¹^ORCID,Talana Chloe Adrienna¹^ORCID,Yang Eun Sung¹^ORCID,Chen Man¹^ORCID,Choe Misook¹^ORCID,Shi Wei¹^ORCID,Teng I-Ting¹,Creanga Adrian¹^ORCID,Jenkins Claudia²,Leung Kwanyee¹^ORCID,Liu Tracy¹,Stancofski Erik-Stephane D.¹,Stephens Tyler²,Zhang Baoshan¹^ORCID,Tsybovsky Yaroslav²,Graham Barney S.¹^ORCID,Mascola John R.¹^ORCID,Sullivan Nancy J.¹^ORCID,Kwong Peter D.¹^ORCID

Affiliation:

1. Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.

2. Electron Microscopy Laboratory, Cancer Research Technology Program, Leidos Biomedical Research, Frederick National Laboratory for Cancer Research, Frederick, MD 21702, USA.

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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