Compounds derived from Humulus lupulus inhibit SARS-CoV-2 papain-like protease and virus replication.

COVID-19 Hop compounds Papain-like protease SARS-CoV-2 Viral proteases Xanthohumol

Journal

Phytomedicine : international journal of phytotherapy and phytopharmacology
ISSN: 1618-095X
Titre abrégé: Phytomedicine
Pays: Germany
ID NLM: 9438794

Informations de publication

Date de publication:
30 Oct 2023
Historique:
received: 04 07 2023
revised: 27 10 2023
accepted: 29 10 2023
medline: 18 11 2023
pubmed: 18 11 2023
entrez: 17 11 2023
Statut: aheadofprint

Résumé

Selected natural compounds exhibit very good antiviral properties. Especially, the medicinal plant Humulus lupulus (hop) contains several secondary plant metabolites some of which have previously shown antiviral activities. Among them, the prenylated chalcone xanthohumol (XN) demonstrated to be a potent inhibitor of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) main protease (M Following the finding that xanthohumol (XN) is a potent inhibitor of SARS-CoV-2 M The modulatory effect of the hop compounds on PL In silico docking analysis was used to predict the binding affinity of hop compounds to the active site of PL Our in silico docking suggests that the purified hop compounds bind to the active site of SARS-CoV-2 PL In addition to the already known inhibition of M

Sections du résumé

BACKGROUND BACKGROUND
Selected natural compounds exhibit very good antiviral properties. Especially, the medicinal plant Humulus lupulus (hop) contains several secondary plant metabolites some of which have previously shown antiviral activities. Among them, the prenylated chalcone xanthohumol (XN) demonstrated to be a potent inhibitor of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) main protease (M
HYPOTHESIS/PURPOSE OBJECTIVE
Following the finding that xanthohumol (XN) is a potent inhibitor of SARS-CoV-2 M
STUDY DESIGN METHODS
The modulatory effect of the hop compounds on PL
METHODS METHODS
In silico docking analysis was used to predict the binding affinity of hop compounds to the active site of PL
RESULTS RESULTS
Our in silico docking suggests that the purified hop compounds bind to the active site of SARS-CoV-2 PL
CONCLUSION CONCLUSIONS
In addition to the already known inhibition of M

Identifiants

pubmed: 37976697
pii: S0944-7113(23)00535-4
doi: 10.1016/j.phymed.2023.155176
pii:
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

155176

Informations de copyright

Copyright © 2023. Published by Elsevier GmbH.

Déclaration de conflit d'intérêts

Declaration of Competing Interest The funders had no role in the collection, analysis, or interpretation of data, in writing of the manuscript, or in the decision to publish the results. The University Hospital of Tübingen is assignee for the following patents (US-9855242-B2, EP2968261A1) concerning the use of hop compounds for an immunomodulation. All authors declare that apart from the above points there are no other conflicts of interest.

Auteurs

Anna-Maria Herzog (AM)

Department of Cellular Microbiology, University of Hohenheim, 70599 Stuttgart, Germany.

Katharina Göbel (K)

Department of Cellular Microbiology, University of Hohenheim, 70599 Stuttgart, Germany.

Luigi Marongiu (L)

Department of Internal Medicine VIII, University Hospital Tuebingen, 72076 Tuebingen, Germany; Department of Nutritional Biochemistry, University of Hohenheim, 70599 Stuttgart, Germany.

Natalia Ruetalo (N)

Institute for Medical Virology and Epidemiology of Viral Diseases, University Hospital Tuebingen, 72076 Tuebingen, Germany.

Marta Campos Alonso (MC)

Institute of Neuropathology, Faculty of Medicine, University of Freiburg, 79106 Freiburg, Germany.

Christian Leischner (C)

Department of Nutritional Biochemistry, University of Hohenheim, 70599 Stuttgart, Germany.

Christian Busch (C)

Dermatologie zum Delfin, 8400 Winterthur, Switzerland.

Markus Burkard (M)

Department of Nutritional Biochemistry, University of Hohenheim, 70599 Stuttgart, Germany.

Ulrich M Lauer (UM)

Department of Internal Medicine VIII, University Hospital Tuebingen, 72076 Tuebingen, Germany.

Paul P Geurink (PP)

Department of Cell and Chemical Biology, Leiden University Medical Center, 2333 ZC Leiden, The Netherlands.

Klaus-Peter Knobeloch (KP)

Institute of Neuropathology, Faculty of Medicine, University of Freiburg, 79106 Freiburg, Germany.

Michael Schindler (M)

Institute for Medical Virology and Epidemiology of Viral Diseases, University Hospital Tuebingen, 72076 Tuebingen, Germany. Electronic address: michael.schindler@med.uni-tuebingen.de.

Günter Fritz (G)

Department of Cellular Microbiology, University of Hohenheim, 70599 Stuttgart, Germany. Electronic address: guenter.fritz@uni-hohenheim.de.

Sascha Venturelli (S)

Department of Nutritional Biochemistry, University of Hohenheim, 70599 Stuttgart, Germany; Institute of Physiology, Department of Vegetative and Clinical Physiology, University Hospital Tuebingen, 72076 Tuebingen, Germany. Electronic address: sascha.venturelli@uni-hohenheim.de.

Classifications MeSH