Antibodies with Potent and Broad Neutralizing Activity against Antigenically Diverse and Highly Transmissible SARS-CoV-2 Variants

Emergence of highly transmissible SARS-CoV-2 variants of concern that are resistant to current therapeutic antibodies highlights the need for continuing discovery of broadly reactive antibodies.

Scientists at the Vaccine Research Center of the National Institute of Allergy and Infectious Diseases discovered and characterized a group of human monoclonal antibodies that target unique epitopes on the receptor binding domain of SARS-CoV-2 spike protein. These antibodies ultra-potently neutralize >12 variants of SARS-CoV-2, including P1, B.1.429, B.1.1.7 and B.1.351, as shown in a pseudovirus neutralization assay. These antibodies target 3 distinct epitopes in the receptor binding domain of the spike protein and function by blocking ACE2 binding. These antibodies are not impacted by spike mutations that knockout binding to other therapeutic antibodies, including E484K, N439K, Y453F, L452R and K417N. Several antibodies are able to simultaneously bind to the spike protein and are compatible for use in combination therapies. In in vitro assays, these combinations were shown to decrease the appearance of escape mutants suggesting the potential to mitigate resistance development when used as combination therapy.

This technology is available for licensing for commercial development in accordance with 35 U.S.C. § 209 and 37 CFR Part 404.