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Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody

Abstract : SARS-CoV-2 is a newly emerged coronavirus responsible for the current COVID-19 pandemic that 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 multiple monoclonal antibodies targeting SARS-CoV-2 S identified from memory B cells of an individual who was infected with 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 S receptor-binding domain. Using cryo-electron microscopy and binding assays, we show that S309 recognizes a glycan-containing epitope that is conserved within the sarbecovirus subgenus, without competing with receptor attachment. Antibody cocktails including S309 along with other antibodies identified here further enhanced SARS-CoV-2 neutralization and may limit the emergence of neutralization-escape mutants. These results pave the way for using S309- and S309-containing antibody cocktails for prophylaxis in individuals at high risk of exposure or as a post-exposure therapy to limit or treat severe disease.
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https://hal-pasteur.archives-ouvertes.fr/pasteur-02623374
Contributor : Maria-Alejandra Tortorici <>
Submitted on : Tuesday, May 26, 2020 - 8:00:05 AM
Last modification on : Thursday, June 18, 2020 - 3:27:05 AM

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Dora Pinto, Young-Jun Park, Martina Beltramello, Alexandra Walls, M. Alejandra Tortorici, et al.. Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody. Nature, Nature Publishing Group, 2020, ⟨10.1038/s41586-020-2349-y⟩. ⟨pasteur-02623374⟩

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