Structural basis and mode of action for two broadly neutralizing antibodies against SARS-CoV-2 emerging variants of concern

Li, Wenwei; Chen, Yaozong; Prévost, Jérémie; Ullah, Irfan; Lu, Maolin; Gong, Shang Yu; Tauzin, Alexandra; Gasser, Romain; Vézina, Dani; Anand, Sai Priya; Goyette, Guillaume; Chaterjee, Debashree; Ding, Shilei; Tolbert, William D.; Grunst, Michael W.; Bo, Yuxia; Zhang, Shijian; Richard, Jonathan; Zhou, Fei; Huang, Rick K.; Esser, Lothar; Zeher, Allison; Côté, Marceline; Kumar, Priti; Sodroski, Joseph; Xia, Di; Uchil, Pradeep D.; Pazgier, Marzena; Finzi, Andrés; Mothes, Walther

doi:10.1016/j.celrep.2021.110210

Title: Structural basis and mode of action for two broadly neutralizing antibodies against SARS-CoV-2 emerging variants of concern

Journal Article · 15 December 2021 · Cell Reports

DOI: https://doi.org/10.1016/j.celrep.2021.110210 · OSTI ID:1981562

Li, Wenwei ^[1]; Chen, Yaozong ^[2]; Prévost, Jérémie ^[3];

^[1];

^[4];

^[3];

^[3]; Vézina, Dani ^[3]; Anand, Sai Priya ^[4];

^[5]; Chaterjee, Debashree ^[5]; Ding, Shilei ^[5]; Tolbert, William D. ^[2];

^[1];

^[6]; Zhang, Shijian ^[7]; Richard, Jonathan ^[3]; Zhou, Fei ^[8]; Huang, Rick K. ^[8] more »

Yale University, New Haven, CT (United States). School of Medicine
Uniformed Services University of the Health Sciences, Bethesda, MD (United States)
Centre de Recherche du CHUM (CRCHUM), Montreal (Canada); University of Montreal, QC (Canada)
Centre de Recherche du CHUM (CRCHUM), Montreal (Canada); McGill University, Montreal, QC (Canada)
Centre de Recherche du CHUM (CRCHUM), Montreal (Canada)
University of Ottawa, ON (Canada)
Dana-Farber Cancer Institute, Boston, MA; Harvard Medical School, Boston, MA (United States)
National Institutes of Health (NIH), Bethesda, MD (United States)
Centre de Recherche du CHUM (CRCHUM), Montreal (Canada); University of Montreal, QC (Canada); McGill University, Montreal, QC (Canada)

Emerging variants of concern for the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) can transmit more efficiently and partially evade protective immune responses, thus necessitating continued refinement of antibody therapies and immunogen design. Here, we elucidate the structural basis and mode of action for two potent SARS-CoV-2 spike (S)-neutralizing monoclonal antibodies, CV3-1 and CV3-25, which remain effective against emerging variants of concern in vitro and in vivo. CV3-1 binds to the (485-GFN-487) loop within the receptor-binding domain (RBD) in the “RBD-up” position and triggers potent shedding of the S1 subunit. In contrast, CV3-25 inhibits membrane fusion by binding to an epitope in the stem helix region of the S2 subunit that is highly conserved among β-coronaviruses. Thus, vaccine immunogen designs that incorporate the conserved regions in the RBD and stem helix region are candidates to elicit pan-coronavirus protective immune responses.

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Research Organization:: SLAC National Accelerator Laboratory, Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL); Yale University, New Haven, CT (United States). School of Medicine

Sponsoring Organization:: Canada Foundation for Innovation (CFI); Canadian Institutes of Health Research (CIHR); Fondation du CHUM; Gruber foundation; National Institutes of Health (NIH); USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: AC02-76SF00515

OSTI ID:: 1981562

Journal Information:: Cell Reports, Journal Name: Cell Reports Journal Issue: 2 Vol. 38; ISSN 2211-1247

Publisher:: ElsevierCopyright Statement

Country of Publication:: United States

Language:: English

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Prospective mapping of viral mutations that escape antibodies used to treat COVID-19 Starr, Tyler N.; Greaney, Allison J.; Addetia, Amin Science, Vol. 371, Issue 6531 https://doi.org/10.1126/science.abf9302	journal	January 2021
Ultrapotent antibodies against diverse and highly transmissible SARS-CoV-2 variants Wang, Lingshu; Zhou, Tongqing; Zhang, Yi Science, Vol. 373, Issue 6556 https://doi.org/10.1126/science.abh1766	journal	July 2021
Defining variant-resistant epitopes targeted by SARS-CoV-2 antibodies: A global consortium study Hastie, Kathryn M.; Li, Haoyang; Bedinger, Daniel Science, Vol. 374, Issue 6566 https://doi.org/10.1126/science.abh2315	journal	October 2021
Effect of natural mutations of SARS-CoV-2 on spike structure, conformation, and antigenicity Gobeil, Sophie M. -C.; Janowska, Katarzyna; McDowell, Shana Science, Vol. 373, Issue 6555 https://doi.org/10.1126/science.abi6226	journal	August 2021
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