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Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody.
Nature. 2020 Jul; 583(7815):290-295.Nat

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.

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Publisher Full Text (DOI)

Authors+Show Affiliations

Pinto D
Humabs BioMed SA, Vir Biotechnology, Bellinzona, Switzerland.
Park YJ
Department of Biochemistry, University of Washington, Seattle, WA, USA.
Beltramello M
Humabs BioMed SA, Vir Biotechnology, Bellinzona, Switzerland.
Walls AC
Department of Biochemistry, University of Washington, Seattle, WA, USA.
Tortorici MA
Department of Biochemistry, University of Washington, Seattle, WA, USA. Institut Pasteur and CNRS UMR 3569, Unité de Virologie Structurale, Paris, France.
Bianchi S
Humabs BioMed SA, Vir Biotechnology, Bellinzona, Switzerland.
Jaconi S
Humabs BioMed SA, Vir Biotechnology, Bellinzona, Switzerland.
Culap K
Humabs BioMed SA, Vir Biotechnology, Bellinzona, Switzerland.
Zatta F
Humabs BioMed SA, Vir Biotechnology, Bellinzona, Switzerland.
De Marco A
Humabs BioMed SA, Vir Biotechnology, Bellinzona, Switzerland.
Peter A
Humabs BioMed SA, Vir Biotechnology, Bellinzona, Switzerland.
Guarino B
Humabs BioMed SA, Vir Biotechnology, Bellinzona, Switzerland.
Spreafico R
Vir Biotechnology, San Francisco, CA, USA.
Cameroni E
Humabs BioMed SA, Vir Biotechnology, Bellinzona, Switzerland.
Case JB
Department of Medicine, Washington University School of Medicine, St Louis, MO, USA.
Chen RE
Department of Medicine, Washington University School of Medicine, St Louis, MO, USA. Department of Pathology and Immunology, Washington University School of Medicine, St Louis, MO, USA.
Havenar-Daughton C
Vir Biotechnology, San Francisco, CA, USA.
Snell G
Vir Biotechnology, San Francisco, CA, USA.
Telenti A
Vir Biotechnology, San Francisco, CA, USA.
Virgin HW
Vir Biotechnology, San Francisco, CA, USA.
Lanzavecchia A
Humabs BioMed SA, Vir Biotechnology, Bellinzona, Switzerland. Institute for Research in Biomedicine, Università della Svizzera Italiana, Bellinzona, Switzerland.
Diamond MS
Department of Medicine, Washington University School of Medicine, St Louis, MO, USA. Department of Pathology and Immunology, Washington University School of Medicine, St Louis, MO, USA. Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO, USA.
Fink K
Humabs BioMed SA, Vir Biotechnology, Bellinzona, Switzerland.
Veesler D
Department of Biochemistry, University of Washington, Seattle, WA, USA. dveesler@uw.edu.
Corti D
Humabs BioMed SA, Vir Biotechnology, Bellinzona, Switzerland. dcorti@vir.bio.

MeSH

Angiotensin-Converting Enzyme 2AnimalsAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralAntibody-Dependent Cell CytotoxicityB-LymphocytesBetacoronavirusCOVID-19Chlorocebus aethiopsCoronavirus InfectionsCross ReactionsCryoelectron MicroscopyEpitopes, B-LymphocyteHEK293 CellsHumansImmune EvasionImmunoglobulin Fab FragmentsImmunologic MemoryKiller Cells, NaturalModels, MolecularNeutralization TestsPandemicsPeptidyl-Dipeptidase APneumonia, ViralSevere acute respiratory syndrome-related coronavirusSARS-CoV-2Severe Acute Respiratory SyndromeSpike Glycoprotein, CoronavirusVero Cells

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

32422645

Citation

Pinto, Dora, et al. "Cross-neutralization of SARS-CoV-2 By a Human Monoclonal SARS-CoV Antibody." Nature, vol. 583, no. 7815, 2020, pp. 290-295.
Pinto D, Park YJ, Beltramello M, et al. Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody. Nature. 2020;583(7815):290-295.
Pinto, D., Park, Y. J., Beltramello, M., Walls, A. C., Tortorici, M. A., Bianchi, S., Jaconi, S., Culap, K., Zatta, F., De Marco, A., Peter, A., Guarino, B., Spreafico, R., Cameroni, E., Case, J. B., Chen, R. E., Havenar-Daughton, C., Snell, G., Telenti, A., ... Corti, D. (2020). Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody. Nature, 583(7815), 290-295. https://doi.org/10.1038/s41586-020-2349-y
Pinto D, et al. Cross-neutralization of SARS-CoV-2 By a Human Monoclonal SARS-CoV Antibody. Nature. 2020;583(7815):290-295. PubMed PMID: 32422645.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody. AU - Pinto,Dora, AU - Park,Young-Jun, AU - Beltramello,Martina, AU - Walls,Alexandra C, AU - Tortorici,M Alejandra, AU - Bianchi,Siro, AU - Jaconi,Stefano, AU - Culap,Katja, AU - Zatta,Fabrizia, AU - De Marco,Anna, AU - Peter,Alessia, AU - Guarino,Barbara, AU - Spreafico,Roberto, AU - Cameroni,Elisabetta, AU - Case,James Brett, AU - Chen,Rita E, AU - Havenar-Daughton,Colin, AU - Snell,Gyorgy, AU - Telenti,Amalio, AU - Virgin,Herbert W, AU - Lanzavecchia,Antonio, AU - Diamond,Michael S, AU - Fink,Katja, AU - Veesler,David, AU - Corti,Davide, Y1 - 2020/05/18/ PY - 2020/4/6/received PY - 2020/5/12/accepted PY - 2020/5/19/pubmed PY - 2020/7/14/medline PY - 2020/5/19/entrez SP - 290 EP - 295 JF - Nature JO - Nature VL - 583 IS - 7815 N2 - 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. SN - 1476-4687 UR - https://www.unboundmedicine.com/medline/citation/32422645/Cross_neutralization_of_SARS_CoV_2_by_a_human_monoclonal_SARS_CoV_antibody_ DB - PRIME DP - Unbound Medicine ER -