An ACE2-blocking antibody confers broad neutralization and protection against Omicron and other SARS-CoV-2 variants
Wenjuan Du; Daniel L. Hurdiss; Dubravka Drabek; Anna Z Mykytyn; Franziska Kaiser; Mariana Gonzalez-Hernandez; Diego Munoz-Santos; Mart M. Lamers; Rien van Haperen; Wentao Li; Ieva Drulyte; Chunyan Wang; Isabel Sola; Federico Armando; Georg Beythien; Malgorzata Ciurkiewicz; Wolfgang Baumgartner; Kate Guilfoyle; Tony Smits; Joline van der Lee; Frank J.M. van Kuppeveld; Geert van Amerongen; Bart L. Haagmans; Luis Enjuanes; Albert DME Osterhaus; Frank Grosveld; Berend Jan Bosch.
Preprint
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| PREPRINT-BIORXIV | ID: ppbiorxiv-480751
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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