A SARS-CoV-2 neutralizing antibody selected from COVID-19 patients binds to the ACE2-RBD interface and is tolerant to most known RBD mutations.
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Authors
Bertoglio, FedericoFühner, Viola
Ruschig, Maximilian
Heine, Philip Alexander
Abassi, Leila
Klünemann, Thomas
Rand, Ulfert
Meier, Doris
Langreder, Nora
Steinke, Stephan
Ballmann, Rico
Schneider, Kai-Thomas
Roth, Kristian Daniel Ralph
Kuhn, Philipp
Riese, Peggy

Schäckermann, Dorina
Korn, Janin
Koch, Allan
Chaudhry, M Zeeshan
Eschke, Kathrin
Kim, Yeonsu
Zock-Emmenthal, Susanne
Becker, Marlies
Scholz, Margitta
Moreira, Gustavo Marçal Schmidt Garcia
Wenzel, Esther Veronika
Russo, Giulio
Garritsen, Hendrikus S P
Casu, Sebastian
Gerstner, Andreas
Roth, Günter
Adler, Julia
Trimpert, Jakob
Hermann, Andreas
Schirrmann, Thomas
Dübel, Stefan
Frenzel, André
van den Heuvel, Joop

Čičin-Šain, Luka
Schubert, Maren
Hust, Michael
Issue Date
2021-07-07
Metadata
Show full item recordAbstract
The novel betacoronavirus severe acute respiratory syndrome-coronavirus-2 (SARS-CoV-2) causes a form of severe pneumonia disease called coronavirus disease 2019 (COVID-19). To develop human neutralizing anti-SARS-CoV-2 antibodies, antibody gene libraries from convalescent COVID-19 patients were constructed and recombinant antibody fragments (scFv) against the receptor-binding domain (RBD) of the spike protein were selected by phage display. The antibody STE90-C11 shows a subnanometer IC50 in a plaque-based live SARS-CoV-2 neutralization assay. The in vivo efficacy of the antibody is demonstrated in the Syrian hamster and in the human angiotensin-converting enzyme 2 (hACE2) mice model. The crystal structure of STE90-C11 Fab in complex with SARS-CoV-2-RBD is solved at 2.0 Å resolution showing that the antibody binds at the same region as ACE2 to RBD. The binding and inhibition of STE90-C11 is not blocked by many known emerging RBD mutations. STE90-C11-derived human IgG1 with FcγR-silenced Fc (COR-101) is undergoing Phase Ib/II clinical trials for the treatment of moderate to severe COVID-19.Citation
Cell Rep. 2021 Jul 27;36(4):109433. doi: 10.1016/j.celrep.2021.109433. Epub 2021 Jul 7.Affiliation
HZI,Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7,38124 Braunschweig, Germany.Publisher
Cell PressJournal
Cell reportsPubMed ID
34273271Type
ArticleLanguage
enEISSN
2211-1247ae974a485f413a2113503eed53cd6c53
10.1016/j.celrep.2021.109433
Scopus Count
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- Creative Commons
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