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            <funder>This work was funded by Toscana Life Sciences, through the European Research Council advanced Grant agreement number 787552 (vAMRes), the European Union’s Horizon 2020 research and innovation program under Grant agreement no. 653316, and the Italian Ministry of Health COVID-2020-12371817 project, under collaborative agreements with The Scripps Research Institute. Work in the O.S. lab is funded by Institut Pasteur, Urgence COVID-19 Fundraising Campaign of Institut Pasteur, ANRS, the Vaccine Research Institute (ANR-10-LABX-77), Labex IBEID (ANR-10-LABX-62-IBEID), ANR/FRM Flash Covid PROTEO-SARS-CoV-2, and IDISCOVR. This work was also funded by the Bill &amp; Melinda Gates Foundation (OPP1170236/INV-004923).</funder>
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                <title level="j">Proceedings of the National Academy of Sciences of the United States of America</title>
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                  <publisher>National Academy of Sciences</publisher>
                  <biblScope unit="volume">119</biblScope>
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                <term xml:lang="en">neutralizing antibody</term>
                <term xml:lang="en">variants of concern</term>
                <term xml:lang="en">monoclonal therapy</term>
                <term xml:lang="en">cryoelectron microscopy</term>
                <term xml:lang="en">SARS-CoV-2</term>
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              <classCode scheme="mesh">Antibody Affinity</classCode>
              <classCode scheme="mesh">COVID-19</classCode>
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              <p>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.</p>
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              <org type="consortium">We thank B. Anderson and H. Turner for microscope assistance, C. Bowman for computational assistance, and G.K. Hedestam and M. Corcoran for scientific discussion regarding human antibody germline genes. We thank Dr. Piet Maes from NRC UZ/KU Leuven (Leuven, Belgium) for kindly providing the Omicron live.</org>
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