The antibody response to SARS-CoV-2 Beta underscores the antigenic distance to other variants
Copyright © 2021 The Author(s). Published by Elsevier Inc. All rights reserved..
Alpha-B.1.1.7, Beta-B.1.351, Gamma-P.1, and Delta-B.1.617.2 variants of SARS-CoV-2 express multiple mutations in the spike protein (S). These may alter the antigenic structure of S, causing escape from natural or vaccine-induced immunity. Beta is particularly difficult to neutralize using serum induced by early pandemic SARS-CoV-2 strains and is most antigenically separated from Delta. To understand this, we generated 674 mAbs from Beta-infected individuals and performed a detailed structure-function analysis of the 27 most potent mAbs: one binding the spike N-terminal domain (NTD), the rest the receptor-binding domain (RBD). Two of these RBD-binding mAbs recognize a neutralizing epitope conserved between SARS-CoV-1 and -2, while 18 target mutated residues in Beta: K417N, E484K, and N501Y. There is a major response to N501Y, including a public IgVH4-39 sequence, with E484K and K417N also targeted. Recognition of these key residues underscores why serum from Beta cases poorly neutralizes early pandemic and Delta viruses.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2022 |
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| Erschienen: |
2022 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:30 |
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| Enthalten in: |
Cell host & microbe - 30(2022), 1 vom: 12. Jan., Seite 53-68.e12 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Liu, Chang [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 24.01.2022 Date Revised 20.03.2024 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.chom.2021.11.013 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| 100 | 1 | |a Liu, Chang |e verfasserin |4 aut | |
| 245 | 1 | 4 | |a The antibody response to SARS-CoV-2 Beta underscores the antigenic distance to other variants |
| 264 | 1 | |c 2022 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ƒaComputermedien |b c |2 rdamedia | ||
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| 500 | |a Date Completed 24.01.2022 | ||
| 500 | |a Date Revised 20.03.2024 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Copyright © 2021 The Author(s). Published by Elsevier Inc. All rights reserved. | ||
| 520 | |a Alpha-B.1.1.7, Beta-B.1.351, Gamma-P.1, and Delta-B.1.617.2 variants of SARS-CoV-2 express multiple mutations in the spike protein (S). These may alter the antigenic structure of S, causing escape from natural or vaccine-induced immunity. Beta is particularly difficult to neutralize using serum induced by early pandemic SARS-CoV-2 strains and is most antigenically separated from Delta. To understand this, we generated 674 mAbs from Beta-infected individuals and performed a detailed structure-function analysis of the 27 most potent mAbs: one binding the spike N-terminal domain (NTD), the rest the receptor-binding domain (RBD). Two of these RBD-binding mAbs recognize a neutralizing epitope conserved between SARS-CoV-1 and -2, while 18 target mutated residues in Beta: K417N, E484K, and N501Y. There is a major response to N501Y, including a public IgVH4-39 sequence, with E484K and K417N also targeted. Recognition of these key residues underscores why serum from Beta cases poorly neutralizes early pandemic and Delta viruses | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a Beta variant | |
| 650 | 4 | |a COVID-19 | |
| 650 | 4 | |a SARS-CoV-2 | |
| 650 | 4 | |a antibody | |
| 650 | 4 | |a immune responses | |
| 650 | 4 | |a neutralization | |
| 650 | 4 | |a receptor-binding domain | |
| 650 | 4 | |a spike protein | |
| 650 | 4 | |a structure | |
| 650 | 4 | |a vaccine | |
| 650 | 7 | |a Antibodies, Monoclonal |2 NLM | |
| 650 | 7 | |a Antibodies, Neutralizing |2 NLM | |
| 650 | 7 | |a Antibodies, Viral |2 NLM | |
| 650 | 7 | |a Spike Glycoprotein, Coronavirus |2 NLM | |
| 700 | 1 | |a Zhou, Daming |e verfasserin |4 aut | |
| 700 | 1 | |a Nutalai, Rungtiwa |e verfasserin |4 aut | |
| 700 | 1 | |a Duyvesteyn, Helen M E |e verfasserin |4 aut | |
| 700 | 1 | |a Tuekprakhon, Aekkachai |e verfasserin |4 aut | |
| 700 | 1 | |a Ginn, Helen M |e verfasserin |4 aut | |
| 700 | 1 | |a Dejnirattisai, Wanwisa |e verfasserin |4 aut | |
| 700 | 1 | |a Supasa, Piyada |e verfasserin |4 aut | |
| 700 | 1 | |a Mentzer, Alexander J |e verfasserin |4 aut | |
| 700 | 1 | |a Wang, Beibei |e verfasserin |4 aut | |
| 700 | 1 | |a Case, James Brett |e verfasserin |4 aut | |
| 700 | 1 | |a Zhao, Yuguang |e verfasserin |4 aut | |
| 700 | 1 | |a Skelly, Donal T |e verfasserin |4 aut | |
| 700 | 1 | |a Chen, Rita E |e verfasserin |4 aut | |
| 700 | 1 | |a Johnson, Sile Ann |e verfasserin |4 aut | |
| 700 | 1 | |a Ritter, Thomas G |e verfasserin |4 aut | |
| 700 | 1 | |a Mason, Chris |e verfasserin |4 aut | |
| 700 | 1 | |a Malik, Tariq |e verfasserin |4 aut | |
| 700 | 1 | |a Temperton, Nigel |e verfasserin |4 aut | |
| 700 | 1 | |a Paterson, Neil G |e verfasserin |4 aut | |
| 700 | 1 | |a Williams, Mark A |e verfasserin |4 aut | |
| 700 | 1 | |a Hall, David R |e verfasserin |4 aut | |
| 700 | 1 | |a Clare, Daniel K |e verfasserin |4 aut | |
| 700 | 1 | |a Howe, Andrew |e verfasserin |4 aut | |
| 700 | 1 | |a Goulder, Philip J R |e verfasserin |4 aut | |
| 700 | 1 | |a Fry, Elizabeth E |e verfasserin |4 aut | |
| 700 | 1 | |a Diamond, Michael S |e verfasserin |4 aut | |
| 700 | 1 | |a Mongkolsapaya, Juthathip |e verfasserin |4 aut | |
| 700 | 1 | |a Ren, Jingshan |e verfasserin |4 aut | |
| 700 | 1 | |a Stuart, David I |e verfasserin |4 aut | |
| 700 | 1 | |a Screaton, Gavin R |e verfasserin |4 aut | |
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