Autor: |
Neil G. Paterson, Rita E. Chen, Elizabeth E. Fry, Alex Fyfe, Christina Dold, Chang Liu, Gavin R. Screaton, Yanchun Peng, Julika Raedecke, Piyada Supasa, Javier Gilbert-Jaramillo, Alexander J. Mentzer, J Slon-Campos, Mark A. Williams, Thomas S. Walter, Guido C. Paesen, Julian C. Knight, Nigel J. Temperton, Donal T. Skelly, Miles W. Carroll, Sunetra Gupta, David I. Stuart, Kuan-Ying A. Huang, Wanwisa Dejnirattisai, Tao Dong, William James, Karen R. Buttigieg, Yuguang Zhao, Tiong Kit Tan, Baoling Ying, David R. Hall, R Levin, A Howe, James Brett Case, C. Alistair Seibert, Michael S. Diamond, Adam L. Bailey, Jingshan Ren, Beibei Wang, Natasha M. Kafai, Felicity K.R. Bertram, Helen M. Ginn, Andrew J. Pollard, Yun Song, Alain Townsend, Helen M. E. Duyvesteyn, Paul Klenerman, Naomi Coombes, Juthathip Mongkolspaya, D. Zhou, Craig Thompson, Cesar Lopez-Camacho, Daniel K. Clare |
Rok vydání: |
2020 |
Předmět: |
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Zdroj: |
Cell |
ISSN: |
1097-4172 0092-8674 |
Popis: |
Antibodies are crucial to immune protection against SARS-CoV-2, with some in emergency use as therapeutics. Here we identify 377 human monoclonal antibodies (mAbs) recognizing the virus spike, and focus mainly on 80 that bind the receptor binding domain (RBD). We devise a competition data driven method to map RBD binding sites. We find that although antibody binding sites are widely dispersed, neutralizing antibody binding is focused, with nearly all highly inhibitory mAbs (IC50 Dejnirattisai et al. present an in-depth study of the human antibody response to SARS-CoV-2 infection. By characterizing 377 human mAbs from recovered COVID-19 patients, and determining 19 protein structures, they construct a map of antibody footprints on the RBD describe in great detail its antigenic anatomy. |
Databáze: |
OpenAIRE |
Externí odkaz: |
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