Author
Listed:
- Dora Pinto
(Vir Biotechnology)
- Young-Jun Park
(University of Washington)
- Martina Beltramello
(Vir Biotechnology)
- Alexandra C. Walls
(University of Washington)
- M. Alejandra Tortorici
(University of Washington
Unité de Virologie Structurale)
- Siro Bianchi
(Vir Biotechnology)
- Stefano Jaconi
(Vir Biotechnology)
- Katja Culap
(Vir Biotechnology)
- Fabrizia Zatta
(Vir Biotechnology)
- Anna De Marco
(Vir Biotechnology)
- Alessia Peter
(Vir Biotechnology)
- Barbara Guarino
(Vir Biotechnology)
- Roberto Spreafico
(Vir Biotechnology)
- Elisabetta Cameroni
(Vir Biotechnology)
- James Brett Case
(Washington University School of Medicine)
- Rita E. Chen
(Washington University School of Medicine
Washington University School of Medicine)
- Colin Havenar-Daughton
(Vir Biotechnology)
- Gyorgy Snell
(Vir Biotechnology)
- Amalio Telenti
(Vir Biotechnology)
- Herbert W. Virgin
(Vir Biotechnology)
- Antonio Lanzavecchia
(Vir Biotechnology
Università della Svizzera Italiana)
- Michael S. Diamond
(Washington University School of Medicine
Washington University School of Medicine
Washington University School of Medicine)
- Katja Fink
(Vir Biotechnology)
- David Veesler
(University of Washington)
- Davide Corti
(Vir Biotechnology)
Abstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a newly emerged coronavirus that is responsible for the current pandemic of coronavirus disease 2019 (COVID-19), which has resulted in more than 3.7 million infections and 260,000 deaths as of 6 May 20201,2. Vaccine and therapeutic discovery efforts are paramount to curb the pandemic spread of this zoonotic virus. The SARS-CoV-2 spike (S) glycoprotein promotes entry into host cells and is the main target of neutralizing antibodies. Here we describe several monoclonal antibodies that target the S glycoprotein of SARS-CoV-2, which we identified from memory B cells of an individual who was infected with severe acute respiratory syndrome coronavirus (SARS-CoV) in 2003. One antibody (named S309) potently neutralizes SARS-CoV-2 and SARS-CoV pseudoviruses as well as authentic SARS-CoV-2, by engaging the receptor-binding domain of the S glycoprotein. Using cryo-electron microscopy and binding assays, we show that S309 recognizes an epitope containing a glycan that is conserved within the Sarbecovirus subgenus, without competing with receptor attachment. Antibody cocktails that include S309 in combination with other antibodies that we identified further enhanced SARS-CoV-2 neutralization, and may limit the emergence of neutralization-escape mutants. These results pave the way for using S309 and antibody cocktails containing S309 for prophylaxis in individuals at a high risk of exposure or as a post-exposure therapy to limit or treat severe disease.
Suggested Citation
Dora Pinto & Young-Jun Park & Martina Beltramello & Alexandra C. Walls & M. Alejandra Tortorici & Siro Bianchi & Stefano Jaconi & Katja Culap & Fabrizia Zatta & Anna De Marco & Alessia Peter & Barbara, 2020.
"Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody,"
Nature, Nature, vol. 583(7815), pages 290-295, July.
Handle:
RePEc:nat:nature:v:583:y:2020:i:7815:d:10.1038_s41586-020-2349-y
DOI: 10.1038/s41586-020-2349-y
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