期刊
CELL
卷 181, 期 5, 页码 1004-+出版社
CELL PRESS
DOI: 10.1016/j.cell.2020.04.031
关键词
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资金
- National Institutes of Health (NIH)/National Institute of Allergy and Infectious Disease (NIAID) [R01-AI127521]
- NIAID
- VIB, Ghent University GOA project
- FWO fellowship
- VLAIO fellowship
- FWOsb fellowship
- FWO-SBO grant GlycoDelete
- BMBF (RAPID consortium) [01K11723D]
- U.S. Department of Energy (DOE), Office of Biological and Environmental Research [DE-AC02-06CH11357]
- FWO-EOS project VIREOS
Coronaviruses make use of a large envelope protein called spike (S) to engage host cell receptors and catalyze membrane fusion. Because of the vital role that these S proteins play, they represent a vulnerable target for the development of therapeutics. Here, we describe the isolation of single-domain antibodies (VHHs) from a llama immunized with prefusion-stabilized coronavirus spikes. These VHHs neutralize MERS-CoV or SARSCoV-1 S pseudotyped viruses, respectively. Crystal structures of these VHHs bound to their respective viral targets reveal two distinct epitopes, but both VHHs interfere with receptor binding. We also show cross-reactivity between the SARS-CoV-1 S-directed VHH and SARS-CoV-2 S and demonstrate that this cross-reactive VHH neutralizes SARS-CoV-2 S pseudotyped viruses as a bivalent human IgG Fc-fusion. These data provide a molecular basis for the neutralization of pathogenic betacoronaviruses by VHHs and suggest that these molecules may serve as useful therapeutics during coronavirus outbreaks.
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