Inhibition of acid sphingomyelinase by ambroxol prevents SARS-CoV-2 entry into epithelial cells.


Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
Historique:
received: 10 01 2021
revised: 15 04 2021
accepted: 21 04 2021
pubmed: 26 4 2021
medline: 14 7 2021
entrez: 25 4 2021
Statut: ppublish

Résumé

The acid sphingomyelinase/ceramide system has been shown to be important for cellular infection with at least some viruses, for instance, rhinovirus or severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Functional inhibition of the acid sphingomyelinase using tricyclic antidepressants prevented infection of epithelial cells, for instance with SARS-CoV-2. The structure of ambroxol, that is, trans-4-[(2,4-dibromanilin-6-yl)-methyamino]-cyclohexanol, a mucolytic drug applied by inhalation, suggests that the drug might inhibit the acid sphingomyelinase and thereby infection with SARS-CoV-2. To test this, we used vesicular stomatitis virus pseudoviral particles presenting SARS-CoV-2 spike protein on their surface (pp-VSV-SARS-CoV-2 spike), a bona fide system for mimicking SARS-CoV-2 entry into cells. Viral uptake and formation of ceramide localization were determined by fluorescence microscopy, activity of the acid sphingomyelinase by consumption of [

Identifiants

pubmed: 33895135
pii: S0021-9258(21)00490-7
doi: 10.1016/j.jbc.2021.100701
pmc: PMC8062550
pii:
doi:

Substances chimiques

Antiviral Agents 0
Ceramides 0
Expectorants 0
Sphingomyelins 0
Spike Glycoprotein, Coronavirus 0
spike protein, SARS-CoV-2 0
Ambroxol 200168S0CL
SMPD1 protein, human EC 3.1.4.12
Sphingomyelin Phosphodiesterase EC 3.1.4.12

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

100701

Informations de copyright

Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.

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Auteurs

Alexander Carpinteiro (A)

Institute of Molecular Biology, University of Duisburg-Essen, Essen, Germany; Department of Hematology, University Hospital Essen, University of Duisburg-Essen, Essen, Germany.

Barbara Gripp (B)

Zentrum für Seelische Gesundheit des Kindes- und Jugendalters, Sana-Klinikum Remscheid GmbH, Remscheid, Germany.

Markus Hoffmann (M)

Infection Biology Unit, German Primate Center - Leibniz Institute for Primate Research, Göttingen, Germany; Faculty of Biology and Psychology, University of Göttingen, Göttingen, Germany.

Stefan Pöhlmann (S)

Infection Biology Unit, German Primate Center - Leibniz Institute for Primate Research, Göttingen, Germany; Faculty of Biology and Psychology, University of Göttingen, Göttingen, Germany.

Nicolas Hoertel (N)

AP-HP.Centre-Université de Paris, Hôpital Corentin-Celton, Département de Psychiatrie, Issy-les-Moulineaux, and Université de Paris, INSERM, Institut de Psychiatrie et Neurosciences de Paris, UMR_S1266, and Faculté de Santé, UFR de Médecine, Paris, France.

Michael J Edwards (MJ)

Department of Surgery, Medical School, University of Cincinnati, Cincinnati, Ohio, USA.

Markus Kamler (M)

Department of Thoracic and Cardiovascular Surgery, Division of Thoracic Transplantation, University Hospital Essen, Essen, Germany.

Johannes Kornhuber (J)

Department of Psychiatry and Psychotherapy, University Hospital of Erlangen, Friedrich-Alexander University Erlangen-Nürnberg (FAU), Erlangen, Germany.

Katrin Anne Becker (KA)

Institute of Molecular Biology, University of Duisburg-Essen, Essen, Germany.

Erich Gulbins (E)

Institute of Molecular Biology, University of Duisburg-Essen, Essen, Germany; Department of Surgery, Medical School, University of Cincinnati, Cincinnati, Ohio, USA. Electronic address: erich.gulbins@uni-due.de.

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Classifications MeSH