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Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529
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 neutral...
Autores principales: | , , , , , , , , , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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American Association for the Advancement of Science
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9580340/ https://www.ncbi.nlm.nih.gov/pubmed/35324257 http://dx.doi.org/10.1126/science.abn8897 |
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author | Zhou, Tongqing Wang, Lingshu Misasi, John Pegu, Amarendra Zhang, Yi Harris, Darcy R. Olia, Adam S. Talana, Chloe Adrienna Yang, Eun Sung Chen, Man Choe, Misook Shi, Wei Teng, I-Ting Creanga, Adrian Jenkins, Claudia Leung, Kwanyee Liu, Tracy Stancofski, Erik-Stephane D. Stephens, Tyler Zhang, Baoshan Tsybovsky, Yaroslav Graham, Barney S. Mascola, John R. Sullivan, Nancy J. Kwong, Peter D. |
author_facet | Zhou, Tongqing Wang, Lingshu Misasi, John Pegu, Amarendra Zhang, Yi Harris, Darcy R. Olia, Adam S. Talana, Chloe Adrienna Yang, Eun Sung Chen, Man Choe, Misook Shi, Wei Teng, I-Ting Creanga, Adrian Jenkins, Claudia Leung, Kwanyee Liu, Tracy Stancofski, Erik-Stephane D. Stephens, Tyler Zhang, Baoshan Tsybovsky, Yaroslav Graham, Barney S. Mascola, John R. Sullivan, Nancy J. Kwong, Peter D. |
author_sort | Zhou, Tongqing |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-9580340 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | American Association for the Advancement of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-95803402022-10-20 Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529 Zhou, Tongqing Wang, Lingshu Misasi, John Pegu, Amarendra Zhang, Yi Harris, Darcy R. Olia, Adam S. Talana, Chloe Adrienna Yang, Eun Sung Chen, Man Choe, Misook Shi, Wei Teng, I-Ting Creanga, Adrian Jenkins, Claudia Leung, Kwanyee Liu, Tracy Stancofski, Erik-Stephane D. Stephens, Tyler Zhang, Baoshan Tsybovsky, Yaroslav Graham, Barney S. Mascola, John R. Sullivan, Nancy J. Kwong, Peter D. Science Research Articles 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. American Association for the Advancement of Science 2022-03-24 /pmc/articles/PMC9580340/ /pubmed/35324257 http://dx.doi.org/10.1126/science.abn8897 Text en Copyright © 2022 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution License 4.0 (CC BY). https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution license (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Articles Zhou, Tongqing Wang, Lingshu Misasi, John Pegu, Amarendra Zhang, Yi Harris, Darcy R. Olia, Adam S. Talana, Chloe Adrienna Yang, Eun Sung Chen, Man Choe, Misook Shi, Wei Teng, I-Ting Creanga, Adrian Jenkins, Claudia Leung, Kwanyee Liu, Tracy Stancofski, Erik-Stephane D. Stephens, Tyler Zhang, Baoshan Tsybovsky, Yaroslav Graham, Barney S. Mascola, John R. Sullivan, Nancy J. Kwong, Peter D. Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529 |
title | Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529 |
title_full | Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529 |
title_fullStr | Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529 |
title_full_unstemmed | Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529 |
title_short | Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529 |
title_sort | structural basis for potent antibody neutralization of sars-cov-2 variants including b.1.1.529 |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9580340/ https://www.ncbi.nlm.nih.gov/pubmed/35324257 http://dx.doi.org/10.1126/science.abn8897 |
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