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Structural insights of a highly potent pan-neutralizing SARS-CoV-2 human monoclonal antibody. 2022
Jonathan L Torres, and
Gabriel Ozorowski, and
Emanuele Andreano, and
Hejun Liu, and
Jeffrey Copps, and
Giulia Piccini, and
Lorena Donnici, and
Matteo Conti, and
Cyril Planchais, and
Delphine Planas, and
Noemi Manganaro, and
Elisa Pantano, and
Ida Paciello, and
Piero Pileri, and
Timothée Bruel, and
Emanuele Montomoli, and
Hugo Mouquet, and
Olivier Schwartz, and
Claudia Sala, and
Raffaele De Francesco, and
Ian A Wilson, and
Rino Rappuoli, and
Andrew B Ward
Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037.
As the coronavirus disease 2019 (COVID-19) pandemic continues, there is a strong need for highly potent monoclonal antibodies (mAbs) that are resistant against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants of concern (VoCs). Here, we evaluate the potency of the previously described mAb J08 against these variants using cell-based assays and delve into the molecular details of the binding interaction using cryoelectron microscopy (cryo-EM) and X-ray crystallography. We show that mAb J08 has low nanomolar affinity against most VoCs and binds high on the receptor binding domain (RBD) ridge, away from many VoC mutations. These findings further validate the phase II/III human clinical trial underway using mAb J08 as a monoclonal therapy.
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