SARS-CoV-2 RBD antibodies that maximize breadth and resistance to escape

Starr, Tyler N.; Czudnochowski, Nadine; Liu, Zhuoming; Zatta, Fabrizia; Park, Young-Jun; Addetia, Amin; Pinto, Dora; Beltramello, Martina; Hernandez, Patrick; Greaney, Allison J.; Marzi, Roberta; Glass, William G.; Zhang, Ivy; Dingens, Adam S.; Bowen, John E.; Tortorici, M. Alejandra; Walls, Alexandra C.; Wojcechowskyj, Jason A.; De Marco, Anna; Rosen, Laura E.; Zhou, Jiayi; Montiel-Ruiz, Martin; Kaiser, Hannah; Dillen, Josh R.; Tucker, Heather; Bassi, Jessica; Silacci-Fregni, Chiara; Housley, Michael P.; di Iulio, Julia; Lombardo, Gloria; Agostini, Maria; Sprugasci, Nicole; Culap, Katja; Jaconi, Stefano; Meury, Marcel; Dellota Jr, Exequiel; Abdelnabi, Rana; Foo, Shi-Yan Caroline; Cameroni, Elisabetta; Stumpf, Spencer; Croll, Tristan I.; Nix, Jay C.; Havenar-Daughton, Colin; Piccoli, Luca; Benigni, Fabio; Neyts, Johan; Telenti, Amalio; Lempp, Florian A.; Pizzuto, Matteo S.; Chodera, John D.; Hebner, Christy M.; Virgin, Herbert W.; Whelan, Sean P. J.; Veesler, David; Corti, Davide; Bloom, Jesse D.; Snell, Gyorgy

doi:10.1038/s41586-021-03807-6

SARS-CoV-2 RBD antibodies that maximize breadth and resistance to escape

Journal Article · Wed Jul 14 00:00:00 EDT 2021 · Nature (London)

DOI:https://doi.org/10.1038/s41586-021-03807-6· OSTI ID:1877606

^[1]; Czudnochowski, Nadine ^[2]; ^[3]; Zatta, Fabrizia ^[4]; ^[5]; Addetia, Amin ^[1]; Pinto, Dora ^[4]; Beltramello, Martina ^[4]; ^[2]; Greaney, Allison J. ^[6]; ^[4]; Glass, William G. ^[7]; Zhang, Ivy ^[8]; ^[1]; ^[5]; ^[5]; ^[5]; Wojcechowskyj, Jason A. ^[2]; De Marco, Anna ^[4]; ^[2] more »

Fred Hutchinson Cancer Research Center, Seattle, WA, (United States)
Vir Biotechnology, San Francisco, CA (United States)
Washington Univ., St. Louis, MO (United States). School of Medicine
Humabs BioMed (Switzerland)
Univ. of Washington, Seattle, WA (United States)
Fred Hutchinson Cancer Research Center, Seattle, WA, (United States); Univ. of Washington, Seattle, WA (United States)
Memorial Sloan Kettering Cancer Center, New York, NY (United States). Sloan Kettering Institute
Memorial Sloan Kettering Cancer Center, New York, NY (United States). Sloan Kettering Institute; Cornell Univ., NY (United States). Weill Medical College
Katholieke Univ. Leuven, (Belgium)
Univ. of Cambridge (United Kingdom)
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Vir Biotechnology, San Francisco, CA (United States); Washington Univ., St. Louis, MO (United States). School of Medicine

An ideal therapeutic anti-SARS-CoV-2 antibody would resist viral escape^1,2,3, have activity against diverse sarbecoviruses^4,5,6,7, and be highly protective through viral neutralization^8,9,10,11 and effector functions^12,13. Understanding how these properties relate to each other and vary across epitopes would aid the development of therapeutic antibodies and guide vaccine design. Here we comprehensively characterize escape, breadth and potency across a panel of SARS-CoV-2 antibodies targeting the receptor-binding domain (RBD). Despite a trade-off between in vitro neutralization potency and breadth of sarbecovirus binding, we identify neutralizing antibodies with exceptional sarbecovirus breadth and a corresponding resistance to SARS-CoV-2 escape. One of these antibodies, S2H97, binds with high affinity across all sarbecovirus clades to a cryptic epitope and prophylactically protects hamsters from viral challenge. Antibodies that target the angiotensin-converting enzyme 2 (ACE2) receptor-binding motif (RBM) typically have poor breadth and are readily escaped by mutations despite high neutralization potency. Nevertheless, we also characterize a potent RBM antibody (S2E12⁸) with breadth across sarbecoviruses related to SARS-CoV-2 and a high barrier to viral escape. These data highlight principles underlying variation in escape, breadth and potency among antibodies that target the RBD, and identify epitopes and features to prioritize for therapeutic development against the current and potential future pandemics.

View Accepted Manuscript (DOE)

Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER); Office of Research Infrastructure Programs (ORIP); National Institute of Allergy and Infectious Diseases (NIAID); National Institute of General Medical Sciences (NIGMS); National Cancer Institute (NCI); National Science Foundation (NSF); Gates Foundation; Wellcome Trust

Grant/Contract Number:: AC02-05CH11231; AC02-76SF00515

OSTI ID:: 1877606

Alternate ID(s):: OSTI ID: 1958126

Journal Information:: Nature (London), Journal Name: Nature (London) Journal Issue: 7874 Vol. 597; ISSN 0028-0836

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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Journal Article · Thu Oct 27 00:00:00 EDT 2022 · Immunity · OSTI ID:2006467

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60 APPLIED LIFE SCIENCES

SARS-CoV-2 RBD antibodies that maximize breadth and resistance to escape

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