Broadly neutralizing antibodies overcome SARS-CoV-2 Omicron antigenic shift View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2021-12-23

AUTHORS

Elisabetta Cameroni, John E. Bowen, Laura E. Rosen, Christian Saliba, Samantha K. Zepeda, Katja Culap, Dora Pinto, Laura A. VanBlargan, Anna De Marco, Julia di Iulio, Fabrizia Zatta, Hannah Kaiser, Julia Noack, Nisar Farhat, Nadine Czudnochowski, Colin Havenar-Daughton, Kaitlin R. Sprouse, Josh R. Dillen, Abigail E. Powell, Alex Chen, Cyrus Maher, Li Yin, David Sun, Leah Soriaga, Jessica Bassi, Chiara Silacci-Fregni, Claes Gustafsson, Nicholas M. Franko, Jenni Logue, Najeeha Talat Iqbal, Ignacio Mazzitelli, Jorge Geffner, Renata Grifantini, Helen Chu, Andrea Gori, Agostino Riva, Olivier Giannini, Alessandro Ceschi, Paolo Ferrari, Pietro E. Cippà, Alessandra Franzetti-Pellanda, Christian Garzoni, Peter J. Halfmann, Yoshihiro Kawaoka, Christy Hebner, Lisa A. Purcell, Luca Piccoli, Matteo Samuele Pizzuto, Alexandra C. Walls, Michael S. Diamond, Amalio Telenti, Herbert W. Virgin, Antonio Lanzavecchia, Gyorgy Snell, David Veesler, Davide Corti

ABSTRACT

The recently emerged SARS-CoV-2 Omicron variant encodes 37 amino acid substitutions in the spike protein, 15 of which are in the receptor-binding domain (RBD), thereby raising concerns about the effectiveness of available vaccines and antibody-based therapeutics. Here we show that the Omicron RBD binds to human ACE2 with enhanced affinity, relative to the Wuhan-Hu-1 RBD, and binds to mouse ACE2. Marked reductions in neutralizing activity were observed against Omicron compared to the ancestral pseudovirus in plasma from convalescent individuals and from individuals who had been vaccinated against SARS-CoV-2, but this loss was less pronounced after a third dose of vaccine. Most monoclonal antibodies that are directed against the receptor-binding motif lost in vitro neutralizing activity against Omicron, with only 3 out of 29 monoclonal antibodies retaining unaltered potency, including the ACE2-mimicking S2K146 antibody1. Furthermore, a fraction of broadly neutralizing sarbecovirus monoclonal antibodies neutralized Omicron through recognition of antigenic sites outside the receptor-binding motif, including sotrovimab2, S2X2593 and S2H974. The magnitude of Omicron-mediated immune evasion marks a major antigenic shift in SARS-CoV-2. Broadly neutralizing monoclonal antibodies that recognize RBD epitopes that are conserved among SARS-CoV-2 variants and other sarbecoviruses may prove key to controlling the ongoing pandemic and future zoonotic spillovers. More... »

PAGES

664-670

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  • Journal

    TITLE

    Nature

    ISSUE

    7898

    VOLUME

    602

    Author Affiliations

  • Humabs Biomed SA, a subsidiary of Vir Biotechnology, Bellinzona, Switzerland
  • Department of Biochemistry, University of Washington, Seattle, WA, USA
  • Vir Biotechnology, San Francisco, CA, USA
  • Department of Medicine, Washington University of School of Medicine, St Louis, MO, USA
  • ATUM, Newark, CA, USA
  • Division of Allergy and Infectious Diseases, University of Washington, Seattle, WA, USA
  • Department of Paediatrics and Child Health, Aga Khan University, Karachi, Pakistan
  • Instituto de Investigaciones Biomédicas en Retrovirus y SIDA (INBIRS), Facultad de Medicina, Universidad de Buenos Aires, Buenos Aires, Argentina
  • National Institute of Molecular Genetics, Milan, Italy
  • Infectious Disease Unit, Fondazione IRCCS Ca’ Granda, Ospedale Maggiore Policlinico, Milan, Italy
  • Department of Biomedical and Clinical Sciences ‘L.Sacco’ (DIBIC), Università di Milano, Milan, Italy
  • Department of Medicine, Ente Ospedaliero Cantonale, Bellinzona, Switzerland
  • Department of Clinical Pharmacology and Toxicology, University Hospital Zurich, Zurich, Switzerland
  • Clinical School, University of New South Wales, Sydney, New South Wales, Australia
  • Faculty of Medicine, University of Zurich, Zurich, Switzerland
  • Clinical Research Unit, Clinica Luganese Moncucco, Lugano, Switzerland
  • Clinic of Internal Medicine and Infectious Diseases, Clinica Luganese Moncucco, Lugano, Switzerland
  • Influenza Research Institute, Department of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin–Madison, Madison, WI, USA
  • The Research Center for Global Viral Diseases, National Center for Global Health and Medicine Research Institute, Tokyo, Japan
  • Howard Hughes Medical Institute, Seattle, WA, USA
  • Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO, USA
  • Department of Internal Medicine, UT Southwestern Medical Center, Dallas, TX, USA
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/s41586-021-04386-2

    DOI

    http://dx.doi.org/10.1038/s41586-021-04386-2

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1144583143

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/35016195


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