Rapid isolation and profiling of a diverse panel of human monoclonal antibodies targeting the SARS-CoV-2 spike protein
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Zost, S.J, et al. Rapid Isolation and Profiling of a Diverse Panel of Human Monoclonal Antibodies Targeting the Sars-cov-2 Spike Protein. Nature Research, 2020. https://doi.org/10.17615/ynxd-y360APA
Zost, S., Gilchuk, P., Chen, R., Case, J., Reidy, J., Trivette, A., Nargi, R., Sutton, R., Suryadevara, N., Chen, E., Binshtein, E., Shrihari, S., Ostrowski, M., Chu, H., Didier, J., Mac Renaris, K., Jones, T., Day, S., Myers, L., Eun Hyung Lee, F., Nguyen, D., Sanz, I., Martinez, D., Rothlauf, P., Bloyet, L., Whelan, S., Baric, R., Thackray, L., Diamond, M., Carnahan, R., & Crowe, J. (2020). Rapid isolation and profiling of a diverse panel of human monoclonal antibodies targeting the SARS-CoV-2 spike protein. Nature Research. https://doi.org/10.17615/ynxd-y360Chicago
Zost, S.J., P Gilchuk, R.E Chen, J.B Case, J.X Reidy, A Trivette, R.S Nargi et al. 2020. Rapid Isolation and Profiling of a Diverse Panel of Human Monoclonal Antibodies Targeting the Sars-Cov-2 Spike Protein. Nature Research. https://doi.org/10.17615/ynxd-y360- Creator
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Zost, S.J.
- Other Affiliation: Vanderbilt University Medical Center
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Gilchuk, P.
- Other Affiliation: Vanderbilt University Medical Center
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Chen, R.E.
- Other Affiliation: Washington University School of Medicine
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Case, J.B.
- Other Affiliation: Washington University School of Medicine
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Reidy, J.X.
- Other Affiliation: Vanderbilt University Medical Center
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Trivette, A.
- Other Affiliation: Vanderbilt University Medical Center
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Nargi, R.S.
- Other Affiliation: Vanderbilt University Medical Center
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Sutton, R.E.
- Other Affiliation: Vanderbilt University Medical Center
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Suryadevara, N.
- Other Affiliation: Vanderbilt University Medical Center
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Chen, E.C.
- Other Affiliation: Vanderbilt University Medical Center
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Binshtein, E.
- Other Affiliation: Vanderbilt University Medical Center
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Shrihari, S.
- Other Affiliation: Washington University School of Medicine
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Ostrowski, M.
- Other Affiliation: University of Toronto
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Chu, H.Y.
- Other Affiliation: University of Washington
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Didier, J.E.
- Other Affiliation: Berkeley Lights, Inc.
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MacRenaris, K.W.
- Other Affiliation: Berkeley Lights, Inc.
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Jones, T.
- Other Affiliation: Vanderbilt University Medical Center
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Day, S.
- Other Affiliation: Vanderbilt University Medical Center
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Myers, L.
- Other Affiliation: Vanderbilt University Medical Center
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Eun-Hyung Lee, F.
- Other Affiliation: Emory University
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Nguyen, D.C.
- Other Affiliation: Emory University
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Sanz, I.
- Other Affiliation: Emory University
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Martinez, D.R.
- Affiliation: Gillings School of Global Public Health, Department of Epidemiology
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Rothlauf, P.W.
- Other Affiliation: Washington University School of Medicine
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Bloyet, L.-M.
- Other Affiliation: Washington University School of Medicine
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Whelan, S.P.J.
- Other Affiliation: Washington University School of Medicine
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Baric, R.S.
- Affiliation: Gillings School of Global Public Health, Department of Epidemiology
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Thackray, L.B.
- Other Affiliation: Washington University School of Medicine
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Diamond, M.S.
- Other Affiliation: Washington University School of Medicine
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Carnahan, R.H.
- Other Affiliation: Vanderbilt University Medical Center
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Crowe, J.E., Jr.
- Other Affiliation: Vanderbilt University Medical Center
- Abstract
- Antibodies are a principal determinant of immunity for most RNA viruses and have promise to reduce infection or disease during major epidemics. The novel coronavirus SARS-CoV-2 has caused a global pandemic with millions of infections and hundreds of thousands of deaths to date1,2. In response, we used a rapid antibody discovery platform to isolate hundreds of human monoclonal antibodies (mAbs) against the SARS-CoV-2 spike (S) protein. We stratify these mAbs into five major classes on the basis of their reactivity to subdomains of S protein as well as their cross-reactivity to SARS-CoV. Many of these mAbs inhibit infection of authentic SARS-CoV-2 virus, with most neutralizing mAbs recognizing the receptor-binding domain (RBD) of S. This work defines sites of vulnerability on SARS-CoV-2 S and demonstrates the speed and robustness of advanced antibody discovery platforms.
- Date of publication
- 2020
- Keyword
- DOI
- Identifier
- PMID 32651581
- http://dx.doi.org/10.1038/s41591-020-0998-x
- Resource type
- Article
- Rights statement
- In Copyright
- Journal title
- Nature Medicine
- Journal volume
- 26
- Journal issue
- 9
- Page start
- 1422
- Page end
- 1427
- Language
- English
- ISSN
- 1078-8956
- Publisher
- Nature Research
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