An ACE2-blocking antibody confers broad neutralization and protection against Omicron and other SARS-CoV-2 variants
Du, W.; Hurdiss, D. L.; Drabek, D.; Mykytyn, A. Z.; Kaiser, F.; Gonzalez-Hernandez, M.; Munoz-Santos, D.; Lamers, M. M.; van Haperen, R.; Li, W.; Drulyte, I.; Wang, C.; Sola, I.; Armando, F.; Beythien, G.; Ciurkiewicz, M.; Baumgartner, W.; Guilfoyle, K.; Smits, T.; van der Lee, J.; van Kuppeveld, F. J. M.; van Amerongen, G.; Haagmans, B. L.; Enjuanes, L.; Osterhaus, A. D.; Grosveld, F.; Bosch, B. J.
Show abstract
The ongoing evolution of SARS-CoV-2 has resulted in the emergence of Omicron, which displays striking immune escape potential. Many of its mutations localize to the spike protein ACE2 receptor-binding domain, annulling the neutralizing activity of most therapeutic monoclonal antibodies. Here we describe a receptor-blocking human monoclonal antibody, 87G7, that retains ultrapotent neutralization against SARS-CoV-2 variants including the Alpha, Beta, Gamma, Delta and Omicron (BA.1/BA.2) Variants-of-Concern (VOCs). Structural analysis reveals that 87G7 targets a patch of hydrophobic residues in the ACE2-binding site that are highly conserved in SARS-CoV-2 variants, explaining its broad neutralization capacity. 87G7 protects mice and/or hamsters against challenge with all current SARS-CoV-2 VOCs. Our findings may aid the development of sustainable antibody-based strategies against COVID-19 that are more resilient to SARS-CoV-2 antigenic diversity. One sentence summaryA human monoclonal antibody confers broad neutralization and protection against Omicron and other SARS-CoV-2 variants
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