COVID-19.рф: ИНФОРМАЦИЯ ПРОТИВ ПАНДЕМИИ

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SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor

M. Hoffmann, H. Kleine-Weber, S. Schroeder, N. Krüger, T. Herrler, S. Erichsen, T. Schiergens, G. Herrler, N. Wu, A. Nitsche, M. Müller, C. Drosten, S. Pöhlmann,
2021
https://doi.org/10.1016/j.cell.2020.02.052

The emerging SARS-coronavirus 2 (SARS-CoV-2) threatens public health. Hoffmann and coworkers show that SARS-CoV-2 infection depends on the host cell factors ACE2 and TMPRSS2 and can be blocked by a clinically proven protease inhibitor. These findings might help to establish options for prevention and treatment. © 2020 Elsevier Inc.The recent emergence of the novel, pathogenic SARS-coronavirus 2 (SARS-CoV-2) in China and its rapid national and international spread pose a global health emergency. Cell entry of coronaviruses depends on binding of the viral spike (S) proteins to cellular receptors and on S protein priming by host cell proteases. Unravelling which cellular factors are used by SARS-CoV-2 for entry might provide insights into viral transmission and reveal therapeutic targets. Here, we demonstrate that SARS-CoV-2 uses the SARS-CoV receptor ACE2 for entry and the serine protease TMPRSS2 for S protein priming. A TMPRSS2 inhibitor approved for clinical use blocked entry and might constitute a treatment option. Finally, we show that the sera from convalescent SARS patients cross-neutralized SARS-2-S-driven entry. Our results reveal important commonalities between SARS-CoV-2 and SARS-CoV infection and identify a potential target for antiviral intervention. © 2020 Elsevier Inc.

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Документы

Источник

Версии

  • 1. Version of Record от 2021-04-27

Метаданные

Об авторах
  • M. Hoffmann
    Infection Biology Unit, German Primate Center – Leibniz Institute for Primate Research, Göttingen, Germany
  • H. Kleine-Weber
    Faculty of Biology and Psychology, University Göttingen, Göttingen, Germany
  • S. Schroeder
    Charité-Universitätsmedizin Berlin, corporate member of Freie Universität Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, Institute of Virology, Berlin, Germany
  • N. Krüger
    German Centre for Infection Research, associated partner Charité, Berlin, Germany
  • T. Herrler
    Institute of Virology, University of Veterinary Medicine Hannover, Hannover, Germany
  • S. Erichsen
    Research Center for Emerging Infections and Zoonoses, University of Veterinary Medicine Hannover, Hannover, Germany
  • T. Schiergens
    BG Unfallklinik Murnau, Murnau, Germany
  • G. Herrler
    Institute for Biomechanics, BG Unfallklinik Murnau, Murnau, Germany
  • N. Wu
    Institute for Biomechanics, Paracelsus Medical University Salzburg, Salzburg, Austria
  • A. Nitsche
    Biobank of the Department of General, Visceral, and Transplant Surgery, Ludwig-Maximilians-University Munich, Munich, Germany
  • M. Müller
    Robert Koch Institute, ZBS 1 Highly Pathogenic Viruses, WHO Collaborating Centre for Emerging Infections and Biological Threats, Berlin, Germany
  • C. Drosten
    Martsinovsky Institute of Medical Parasitology, Tropical and Vector Borne Diseases, Sechenov University, Moscow, Russian Federation
  • S. Pöhlmann
Название журнала
  • Cell
Том
  • 181
Выпуск
  • 2
Страницы
  • 271-280.e8
Ключевые слова
  • angiotensin converting enzyme 2; camostat mesilate; neutralizing antibody; serine protease TMPRSS2; serine proteinase; unclassified drug; virus spike protein; (3-ethoxycarbonyloxirane-2-carbonyl)leucine (3-methylbutyl) amide; ammonium chloride; angiotensin converting enzyme 2; camostat; coronavirus spike glycoprotein; dipeptidyl carboxypeptidase; gabexate; leucine; neutralizing antibody; proteinase inhibitor; serine proteinase; spike glycoprotein, SARS-CoV; TMPRSS2 protein, human; virus antibody; virus receptor; animal cell; antibody response; Article; controlled study; coronavirus disease 2019; coronavirus disease 2019; Coronavirus infection; human; human cell; mouse; nonhuman; priority journal; protein degradation; SARS coronavirus; SARS-related coronavirus; severe acute respiratory syndrome; Severe acute respiratory syndrome coronavirus 2; virus entry; virus neutralization; virus spike; animal; Betacoronavirus; cell line; chemistry; Coronavirinae; Coronavirus infection; drug development; drug effect; genetics; immunology; metabolism; pandemic; passive immunization; physiology; Vesiculovirus; virus entry; virus pneumonia; Ammonium Chloride; Animals; Antibodies, Neutralizing; Antibodies, Viral; Betacoronavirus; Cell Line; Coronavirus; Coronavirus Infections; Drug Development; Gabexate; Humans; Immunization, Passive; Leucine; Pandemics; Peptidyl-Dipeptidase A; Pneumonia, Viral; Protease Inhibitors; Receptors, Virus; SARS Virus; Serine Endopeptidases; Spike Glycoprotein, Coronavirus; Vesiculovirus; Virus Internalization
Издатель
  • Cell Press
Тип документа
  • journal article
Тип лицензии Creative Commons
  • CC BY-NC-ND
Правовой статус документа
  • Свободная лицензия
Источник
  • scopus
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