An infectious SARS-CoV-2 B.1.1.529 Omicron virus escapes neutralization by therapeutic monoclonal antibodies

The emergence of the highly transmissible B.1.1.529 Omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is concerning for antibody countermeasure efficacy because of the number of mutations in the spike protein. In this study, we tested a panel of anti-receptor-binding do...

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Published in	Nature medicine Vol. 28; no. 3; pp. 490 - 495
Main Authors	VanBlargan, Laura A., Errico, John M., Halfmann, Peter J., Zost, Seth J., Crowe, James E., Purcell, Lisa A., Kawaoka, Yoshihiro, Corti, Davide, Fremont, Daved H., Diamond, Michael S.
Format	Journal Article
Language	English
Published	New York Nature Publishing Group US 01.03.2022 Nature Publishing Group
Subjects	631/326/596/2558 631/326/596/4130 Antibodies, Monoclonal - pharmacology Antibodies, Monoclonal - therapeutic use Antibodies, Monoclonal, Humanized Antibodies, Neutralizing - therapeutic use Antibodies, Viral - therapeutic use Biomedical and Life Sciences Biomedicine Biotechnology Cancer Research Coronaviruses COVID-19 COVID-19 Drug Treatment Humans Immunoglobulin G Infectious Diseases Metabolic Diseases Molecular Medicine Monoclonal antibodies Mutation Neurosciences Neutralization SARS-CoV-2 Severe acute respiratory syndrome coronavirus 2 Spike Glycoprotein, Coronavirus - genetics Spike protein Viral diseases Viruses
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Abstract	The emergence of the highly transmissible B.1.1.529 Omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is concerning for antibody countermeasure efficacy because of the number of mutations in the spike protein. In this study, we tested a panel of anti-receptor-binding domain monoclonal antibodies (mAbs) corresponding to those in clinical use by Vir Biotechnology (S309, the parent mAb of VIR-7831 (sotrovimab)), AstraZeneca (COV2-2196 and COV2-2130, the parent mAbs of AZD8895 and AZD1061), Regeneron (REGN10933 and REGN10987), Eli Lilly (LY-CoV555 and LY-CoV016) and Celltrion (CT-P59) for their ability to neutralize an infectious B.1.1.529 Omicron isolate. Several mAbs (LY-CoV555, LY-CoV016, REGN10933, REGN10987 and CT-P59) completely lost neutralizing activity against B.1.1.529 virus in both Vero-TMPRSS2 and Vero-hACE2-TMPRSS2 cells, whereas others were reduced (COV2-2196 and COV2-2130 combination, ~12-fold decrease) or minimally affected (S309). Our results suggest that several, but not all, of the antibodies in clinical use might lose efficacy against the B.1.1.529 Omicron variant. New in vitro data suggest that the new SARS-CoV-2 Omicron variant is likely to escape neutralization by most therapeutic antibodies currently available.
AbstractList	The emergence of the highly transmissible B.1.1.529 Omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is concerning for antibody countermeasure efficacy because of the number of mutations in the spike protein. In this study, we tested a panel of anti-receptor-binding domain monoclonal antibodies (mAbs) corresponding to those in clinical use by Vir Biotechnology (S309, the parent mAb of VIR-7831 (sotrovimab)), AstraZeneca (COV2-2196 and COV2-2130, the parent mAbs of AZD8895 and AZD1061), Regeneron (REGN10933 and REGN10987), Eli Lilly (LY-CoV555 and LY-CoV016) and Celltrion (CT-P59) for their ability to neutralize an infectious B.1.1.529 Omicron isolate. Several mAbs (LY-CoV555, LY-CoV016, REGN10933, REGN10987 and CT-P59) completely lost neutralizing activity against B.1.1.529 virus in both Vero-TMPRSS2 and Vero-hACE2-TMPRSS2 cells, whereas others were reduced (COV2-2196 and COV2-2130 combination, ~12-fold decrease) or minimally affected (S309). Our results suggest that several, but not all, of the antibodies in clinical use might lose efficacy against the B.1.1.529 Omicron variant. The emergence of the highly transmissible B.1.1.529 Omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is concerning for antibody countermeasure efficacy because of the number of mutations in the spike protein. In this study, we tested a panel of anti-receptor-binding domain monoclonal antibodies (mAbs) corresponding to those in clinical use by Vir Biotechnology (S309, the parent mAb of VIR-7831 (sotrovimab)), AstraZeneca (COV2-2196 and COV2-2130, the parent mAbs of AZD8895 and AZD1061), Regeneron (REGN10933 and REGN10987), Eli Lilly (LY-CoV555 and LY-CoV016) and Celltrion (CT-P59) for their ability to neutralize an infectious B.1.1.529 Omicron isolate. Several mAbs (LY-CoV555, LY-CoV016, REGN10933, REGN10987 and CT-P59) completely lost neutralizing activity against B.1.1.529 virus in both Vero-TMPRSS2 and Vero-hACE2-TMPRSS2 cells, whereas others were reduced (COV2-2196 and COV2-2130 combination, ~12-fold decrease) or minimally affected (S309). Our results suggest that several, but not all, of the antibodies in clinical use might lose efficacy against the B.1.1.529 Omicron variant.The emergence of the highly transmissible B.1.1.529 Omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is concerning for antibody countermeasure efficacy because of the number of mutations in the spike protein. In this study, we tested a panel of anti-receptor-binding domain monoclonal antibodies (mAbs) corresponding to those in clinical use by Vir Biotechnology (S309, the parent mAb of VIR-7831 (sotrovimab)), AstraZeneca (COV2-2196 and COV2-2130, the parent mAbs of AZD8895 and AZD1061), Regeneron (REGN10933 and REGN10987), Eli Lilly (LY-CoV555 and LY-CoV016) and Celltrion (CT-P59) for their ability to neutralize an infectious B.1.1.529 Omicron isolate. Several mAbs (LY-CoV555, LY-CoV016, REGN10933, REGN10987 and CT-P59) completely lost neutralizing activity against B.1.1.529 virus in both Vero-TMPRSS2 and Vero-hACE2-TMPRSS2 cells, whereas others were reduced (COV2-2196 and COV2-2130 combination, ~12-fold decrease) or minimally affected (S309). Our results suggest that several, but not all, of the antibodies in clinical use might lose efficacy against the B.1.1.529 Omicron variant. The emergence of the highly transmissible B.1.1.529 Omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is concerning for antibody countermeasure efficacy because of the number of mutations in the spike protein. In this study, we tested a panel of anti-receptor-binding domain monoclonal antibodies (mAbs) corresponding to those in clinical use by Vir Biotechnology (S309, the parent mAb of VIR-7831 (sotrovimab)), AstraZeneca (COV2-2196 and COV2-2130, the parent mAbs of AZD8895 and AZD1061), Regeneron (REGN10933 and REGN10987), Eli Lilly (LY-CoV555 and LY-CoV016) and Celltrion (CT-P59) for their ability to neutralize an infectious B.1.1.529 Omicron isolate. Several mAbs (LY-CoV555, LY-CoV016, REGN10933, REGN10987 and CT-P59) completely lost neutralizing activity against B.1.1.529 virus in both Vero-TMPRSS2 and Vero-hACE2-TMPRSS2 cells, whereas others were reduced (COV2-2196 and COV2-2130 combination, ~12-fold decrease) or minimally affected (S309). Our results suggest that several, but not all, of the antibodies in clinical use might lose efficacy against the B.1.1.529 Omicron variant.New in vitro data suggest that the new SARS-CoV-2 Omicron variant is likely to escape neutralization by most therapeutic antibodies currently available. The emergence of the highly transmissible B.1.1.529 Omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is concerning for antibody countermeasure efficacy because of the number of mutations in the spike protein. In this study, we tested a panel of anti-receptor-binding domain monoclonal antibodies (mAbs) corresponding to those in clinical use by Vir Biotechnology (S309, the parent mAb of VIR-7831 (sotrovimab)), AstraZeneca (COV2-2196 and COV2-2130, the parent mAbs of AZD8895 and AZD1061), Regeneron (REGN10933 and REGN10987), Eli Lilly (LY-CoV555 and LY-CoV016) and Celltrion (CT-P59) for their ability to neutralize an infectious B.1.1.529 Omicron isolate. Several mAbs (LY-CoV555, LY-CoV016, REGN10933, REGN10987 and CT-P59) completely lost neutralizing activity against B.1.1.529 virus in both Vero-TMPRSS2 and Vero-hACE2-TMPRSS2 cells, whereas others were reduced (COV2-2196 and COV2-2130 combination, ~12-fold decrease) or minimally affected (S309). Our results suggest that several, but not all, of the antibodies in clinical use might lose efficacy against the B.1.1.529 Omicron variant. New in vitro data suggest that the new SARS-CoV-2 Omicron variant is likely to escape neutralization by most therapeutic antibodies currently available.
Author	Errico, John M. Zost, Seth J. Kawaoka, Yoshihiro Crowe, James E. Corti, Davide Diamond, Michael S. Purcell, Lisa A. VanBlargan, Laura A. Halfmann, Peter J. Fremont, Daved H.
Author_xml	– sequence: 1 givenname: Laura A. orcidid: 0000-0002-8922-8946 surname: VanBlargan fullname: VanBlargan, Laura A. organization: Department of Medicine, Washington University School of Medicine – sequence: 2 givenname: John M. orcidid: 0000-0002-4452-8152 surname: Errico fullname: Errico, John M. organization: Department of Pathology & Immunology, Washington University School of Medicine – sequence: 3 givenname: Peter J. surname: Halfmann fullname: Halfmann, Peter J. organization: Influenza Research Institute, Department of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin-Madison – sequence: 4 givenname: Seth J. orcidid: 0000-0001-6712-5076 surname: Zost fullname: Zost, Seth J. organization: Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Department of Pediatrics, Vanderbilt University Medical Center – sequence: 5 givenname: James E. orcidid: 0000-0002-0049-1079 surname: Crowe fullname: Crowe, James E. organization: Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Department of Pediatrics, Vanderbilt University Medical Center, Department of Pathology, and Microbiology and Immunology, Vanderbilt University Medical Center – sequence: 6 givenname: Lisa A. surname: Purcell fullname: Purcell, Lisa A. organization: Vir Biotechnology – sequence: 7 givenname: Yoshihiro orcidid: 0000-0001-5061-8296 surname: Kawaoka fullname: Kawaoka, Yoshihiro organization: Influenza Research Institute, Department of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin-Madison, Division of Virology, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, The Research Center for Global Viral Diseases, National Center for Global Health and Medicine Research Institute – sequence: 8 givenname: Davide orcidid: 0000-0002-5797-1364 surname: Corti fullname: Corti, Davide organization: Humabs BioMed SA, a subsidiary of Vir Biotechnology – sequence: 9 givenname: Daved H. orcidid: 0000-0002-8544-2689 surname: Fremont fullname: Fremont, Daved H. organization: Department of Pathology & Immunology, Washington University School of Medicine, Department of Molecular Microbiology, Washington University School of Medicine, Department of Biochemistry & Molecular Biophysics, Washington University School of Medicine – sequence: 10 givenname: Michael S. orcidid: 0000-0002-8791-3165 surname: Diamond fullname: Diamond, Michael S. email: mdiamond@wustl.edu organization: Department of Medicine, Washington University School of Medicine, Department of Pathology & Immunology, Washington University School of Medicine, Department of Molecular Microbiology, Washington University School of Medicine, Andrew M. and Jane M. Bursky Center for Human Immunology and Immunotherapy Programs, Washington University School of Medicine, Center for Vaccines and Immunity to Microbial Pathogens, Washington University School of Medicine
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/35046573$$D View this record in MEDLINE/PubMed
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ContentType	Journal Article
Copyright	The Author(s), under exclusive licence to Springer Nature America, Inc. 2022 2022. The Author(s), under exclusive licence to Springer Nature America, Inc. The Author(s), under exclusive licence to Springer Nature America, Inc. 2022.
Copyright_xml	– notice: The Author(s), under exclusive licence to Springer Nature America, Inc. 2022 – notice: 2022. The Author(s), under exclusive licence to Springer Nature America, Inc. – notice: The Author(s), under exclusive licence to Springer Nature America, Inc. 2022.
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Snippet	The emergence of the highly transmissible B.1.1.529 Omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is concerning for antibody...
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SubjectTerms	631/326/596/2558 631/326/596/4130 Antibodies, Monoclonal - pharmacology Antibodies, Monoclonal - therapeutic use Antibodies, Monoclonal, Humanized Antibodies, Neutralizing - therapeutic use Antibodies, Viral - therapeutic use Biomedical and Life Sciences Biomedicine Biotechnology Cancer Research Coronaviruses COVID-19 COVID-19 Drug Treatment Humans Immunoglobulin G Infectious Diseases Metabolic Diseases Molecular Medicine Monoclonal antibodies Mutation Neurosciences Neutralization SARS-CoV-2 Severe acute respiratory syndrome coronavirus 2 Spike Glycoprotein, Coronavirus - genetics Spike protein Viral diseases Viruses
Title	An infectious SARS-CoV-2 B.1.1.529 Omicron virus escapes neutralization by therapeutic monoclonal antibodies
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