Abstract
The coronavirus disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) presents a global health emergency that is in urgent need of intervention1,2,3. The entry of SARS-CoV-2 into its target cells depends on binding between the receptor-binding domain (RBD) of the viral spike protein and its cellular receptor, angiotensin-converting enzyme 2 (ACE2)2,4,5,6. Here we report the isolation and characterization of 206 RBD-specific monoclonal antibodies derived from single B cells from 8 individuals infected with SARS-CoV-2. We identified antibodies that potently neutralize SARS-CoV-2; this activity correlates with competition with ACE2 for binding to RBD. Unexpectedly, the anti-SARS-CoV-2 antibodies and the infected plasma did not cross-react with the RBDs of SARS-CoV or Middle East respiratory syndrome-related coronavirus (MERS-CoV), although there was substantial plasma cross-reactivity to their trimeric spike proteins. Analysis of the crystal structure of RBD-bound antibody revealed that steric hindrance inhibits viral engagement with ACE2, thereby blocking viral entry. These findings suggest that anti-RBD antibodies are largely viral-species-specific inhibitors. The antibodies identified here may be candidates for development of clinical interventions against SARS-CoV-2.
【초록키워드】 COVID-19, coronavirus disease, SARS-CoV-2, ACE2, coronavirus, pandemic, antibody, SARS-CoV, monoclonal antibody, Intervention, Proteins, MERS-CoV, angiotensin-converting enzyme 2, inhibitors, viral entry, cross-reactivity, anti-SARS-CoV-2 antibody, RBD, Isolation, plasma, binding, Middle East, Anti-RBD antibody, target cell, health emergency, viral spike protein, acute respiratory syndrome, individual, candidate, trimeric spike, cellular receptor, neutralize, steric hindrance, caused, inhibit, the RBD, the receptor-binding domain, cross-react, entry of SARS-CoV-2, infected with SARS-CoV-2, single B cell, 【제목키워드】 neutralizing antibody, SARS-COV-2 infection, Human, elicited,