期刊
CELL REPORTS
卷 36, 期 4, 页码 -出版社
CELL PRESS
DOI: 10.1016/j.celrep.2021.109433
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- MWK Niedersachsen [14-76103-184CORONA-2/20]
- European Union [101003650]
- Deutsche Herzstiftung
Researchers have developed a human neutralizing antibody against SARS-CoV-2, which shows promising efficacy in animal models and is currently undergoing clinical trials for the treatment of moderate to severe COVID-19. The antibody binds to the receptor-binding domain (RBD) of the spike protein to inhibit the virus, and is not affected by many known RBD mutations.
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 antiSARS-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 angstrom 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 Fc gamma R-silenced Fc (COR-101) is undergoing Phase Ib/II clinical trials for the treatment of moderate to severe COVID-19.
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