Reduced mitochondrial resilience enables non-canonical induction of apoptosis after TNF receptor signaling in virus-infected hepatocytes.


Journal

Journal of hepatology
ISSN: 1600-0641
Titre abrégé: J Hepatol
Pays: Netherlands
ID NLM: 8503886

Informations de publication

Date de publication:
12 2020
Historique:
received: 05 03 2020
revised: 29 05 2020
accepted: 15 06 2020
pubmed: 1 7 2020
medline: 12 11 2021
entrez: 30 6 2020
Statut: ppublish

Résumé

Selective elimination of virus-infected hepatocytes occurs through virus-specific CD8 T cells recognizing peptide-loaded MHC molecules. Herein, we report that virus-infected hepatocytes are also selectively eliminated through a cell-autonomous mechanism. We generated recombinant adenoviruses and genetically modified mouse models to identify the molecular mechanisms determining TNF-induced hepatocyte apoptosis in vivo and used in vivo bioluminescence imaging, immunohistochemistry, immunoblot analysis, RNAseq/proteome/phosphoproteome analyses, bioinformatic analyses, mitochondrial function tests. We found that TNF precisely eliminated only virus-infected hepatocytes independently of local inflammation and activation of immune sensory receptors. TNF receptor I was equally relevant for NF-kB activation in healthy and infected hepatocytes, but selectively mediated apoptosis in infected hepatocytes. Caspase 8 activation downstream of TNF receptor signaling was dispensable for apoptosis in virus-infected hepatocytes, indicating an unknown non-canonical cell-intrinsic pathway promoting apoptosis in hepatocytes. We identified a unique state of mitochondrial vulnerability in virus-infected hepatocytes as the cause for this non-canonical induction of apoptosis through TNF. Mitochondria from virus-infected hepatocytes showed normal biophysical and bioenergetic functions but were characterized by reduced resilience to calcium challenge. In the presence of unchanged TNF-induced signaling, reactive oxygen species-mediated calcium release from the endoplasmic reticulum caused mitochondrial permeability transition and apoptosis, which identified a link between extrinsic death receptor signaling and cell-intrinsic mitochondrial-mediated caspase activation. Our findings reveal a novel concept in immune surveillance by identifying a cell-autonomous defense mechanism that selectively eliminates virus-infected hepatocytes through mitochondrial permeability transition. The liver is known for its unique immune functions. Herein, we identify a novel mechanism by which virus-infected hepatocytes can selectively eliminate themselves through reduced mitochondrial resilience to calcium challenge.

Sections du résumé

BACKGROUND & AIMS
Selective elimination of virus-infected hepatocytes occurs through virus-specific CD8 T cells recognizing peptide-loaded MHC molecules. Herein, we report that virus-infected hepatocytes are also selectively eliminated through a cell-autonomous mechanism.
METHODS
We generated recombinant adenoviruses and genetically modified mouse models to identify the molecular mechanisms determining TNF-induced hepatocyte apoptosis in vivo and used in vivo bioluminescence imaging, immunohistochemistry, immunoblot analysis, RNAseq/proteome/phosphoproteome analyses, bioinformatic analyses, mitochondrial function tests.
RESULTS
We found that TNF precisely eliminated only virus-infected hepatocytes independently of local inflammation and activation of immune sensory receptors. TNF receptor I was equally relevant for NF-kB activation in healthy and infected hepatocytes, but selectively mediated apoptosis in infected hepatocytes. Caspase 8 activation downstream of TNF receptor signaling was dispensable for apoptosis in virus-infected hepatocytes, indicating an unknown non-canonical cell-intrinsic pathway promoting apoptosis in hepatocytes. We identified a unique state of mitochondrial vulnerability in virus-infected hepatocytes as the cause for this non-canonical induction of apoptosis through TNF. Mitochondria from virus-infected hepatocytes showed normal biophysical and bioenergetic functions but were characterized by reduced resilience to calcium challenge. In the presence of unchanged TNF-induced signaling, reactive oxygen species-mediated calcium release from the endoplasmic reticulum caused mitochondrial permeability transition and apoptosis, which identified a link between extrinsic death receptor signaling and cell-intrinsic mitochondrial-mediated caspase activation.
CONCLUSION
Our findings reveal a novel concept in immune surveillance by identifying a cell-autonomous defense mechanism that selectively eliminates virus-infected hepatocytes through mitochondrial permeability transition.
LAY SUMMARY
The liver is known for its unique immune functions. Herein, we identify a novel mechanism by which virus-infected hepatocytes can selectively eliminate themselves through reduced mitochondrial resilience to calcium challenge.

Identifiants

pubmed: 32598967
pii: S0168-8278(20)30398-6
doi: 10.1016/j.jhep.2020.06.026
pii:
doi:

Substances chimiques

Receptors, Tumor Necrosis Factor, Type I 0
Tumor Necrosis Factor-alpha 0
Caspase 8 EC 3.4.22.-

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

1347-1359

Informations de copyright

Copyright © 2020 European Association for the Study of the Liver. Published by Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Conflict of interest The authors declare no conflicts of interest that pertain to this work. Please refer to the accompanying ICMJE disclosure forms for further details.

Auteurs

Sandra Lampl (S)

Institute of Molecular Immunology and Experimental Oncology, University Hospital München rechts der Isar; Technical University of Munich, Munich, Germany.

Marianne K Janas (MK)

Institute of Molecular Immunology and Experimental Oncology, University Hospital München rechts der Isar; Technical University of Munich, Munich, Germany.

Sainitin Donakonda (S)

Institute of Molecular Immunology and Experimental Oncology, University Hospital München rechts der Isar; Technical University of Munich, Munich, Germany.

Marcus Brugger (M)

Institute of Molecular Immunology and Experimental Oncology, University Hospital München rechts der Isar; Technical University of Munich, Munich, Germany.

Kerstin Lohr (K)

Institute of Molecular Immunology and Experimental Oncology, University Hospital München rechts der Isar; Technical University of Munich, Munich, Germany.

Annika Schneider (A)

Institute of Molecular Immunology and Experimental Oncology, University Hospital München rechts der Isar; Technical University of Munich, Munich, Germany.

Katrin Manske (K)

Institute of Molecular Immunology and Experimental Oncology, University Hospital München rechts der Isar; Technical University of Munich, Munich, Germany.

Laura E Sperl (LE)

Institute of Structural Biology, Helmholtz Zentrum Munich, Neuherberg, Germany.

Susan Kläger (S)

Structural Membrane Biochemistry, Bavarian NMR Center at the Department of Chemistry and Institute for Advanced Study, Technical University of Munich, Garching, Germany.

Bernhard Küster (B)

Structural Membrane Biochemistry, Bavarian NMR Center at the Department of Chemistry and Institute for Advanced Study, Technical University of Munich, Garching, Germany.

Jennifer Wettmarshausen (J)

Institute for Obesity and Diabetes, Helmholtz Zentrum München, Neuherberg, Germany.

Constanze Müller (C)

Research Unit Analytical Biogeochemistry, Helmholtz Zentrum München, Neuherberg, Germany.

Melanie Laschinger (M)

Clinic of Surgery, University Hospital München rechts der Isar; Technical University of Munich, Munich, Germany.

Daniel Hartmann (D)

Clinic of Surgery, University Hospital München rechts der Isar; Technical University of Munich, Munich, Germany.

Norber Hüser (N)

Clinic of Surgery, University Hospital München rechts der Isar; Technical University of Munich, Munich, Germany.

Fabiana Perocchi (F)

Research Unit Analytical Biogeochemistry, Helmholtz Zentrum München, Neuherberg, Germany; Munich Cluster for Systems Neurology, Munich, Germany.

Philippe Schmitt-Kopplin (P)

Research Unit Analytical Biogeochemistry, Helmholtz Zentrum München, Neuherberg, Germany; Chair of Analytical Food Chemistry, Technical University of Munich, Freising-Weihenstephan, Germany.

Franz Hagn (F)

Institute of Structural Biology, Helmholtz Zentrum Munich, Neuherberg, Germany; Structural Membrane Biochemistry, Bavarian NMR Center at the Department of Chemistry and Institute for Advanced Study, Technical University of Munich, Garching, Germany.

Lars Zender (L)

Division of Gastroenterology and Oncology, University Hospital Tübingen, Tübingen, Germany.

Veit Hornung (V)

Center for Integrated Protein Science (CIPSM), Gene Center and Department of Biochemistry, Ludwig-Maximilians-Universität München, München, Germany.

Christoph Borner (C)

Institute of Molecular Medicine and Cell Research, Faculty of Medicine, University of Freiburg, Freiburg, Germany.

Andreas Pichlmair (A)

Institute of Virology, Technical University of Munich, Munich, Germany.

Hamid Kashkar (H)

Cologne Excellence Cluster on Cellular Stress Response in Aging-Associated Diseases, University of Cologne, Cologne, Germany; Institute for Microbiology and Hygiene, and Center of Molecular Medicine, University of Cologne, Cologne, Germany.

Martin Klingenspor (M)

Molecular Nutritional Medicine, Else Kröner-Fresenius Center, Technical University of Munich, Freising-Weihenstephan, Germany.

Marco Prinz (M)

Institute of Neuropathology, Medical Faculty, University of Freiburg, Germany.

Sabrina Schreiner (S)

Institute of Virology, Helmholtz-Zentrum München, Neuherberg, Germany.

Marcus Conrad (M)

Institute of Metabolism and Cell Death, Helmhotz Zentrum MUnich, Neuherberg, Germany.

Philipp J Jost (PJ)

III. Medical Department for Hematology and Oncology, Klinikum rechts der Isar, Technical University of Munich, Munich, Germany.

Hans Zischka (H)

Institute of Molecular Toxicology and Pharmacology, Helmholtz Zentrum München/German Research Center for Environmental Health GmbH, Neuherberg, Germany; Institute of Toxicology and Environmental Hygiene, School of Medicine, Technical University of Munich, Munich, Germany.

Katja Steiger (K)

Institute of Pathology, Technical University of Munich, Munich, Germany.

Martin Krönke (M)

Cologne Excellence Cluster on Cellular Stress Response in Aging-Associated Diseases, University of Cologne, Cologne, Germany; Institute for Microbiology and Hygiene, and Center of Molecular Medicine, University of Cologne, Cologne, Germany.

Dietmar Zehn (D)

Institute of Physiology and Immunology, Technical University of Munich, Freising-Weihenstephan, Germany.

Ulrike Protzer (U)

Institute of Virology, Technical University of Munich, Munich, Germany; Institute of Virology, Helmholtz-Zentrum München, Neuherberg, Germany; German Center for Infection research (DZIF), Munich Partner Site, Germany.

Mathias Heikenwälder (M)

Institute of Chronic Inflammation and Cancer, German-Cancer-Research Center, Heidelberg, Germany.

Percy A Knolle (PA)

Institute of Molecular Immunology and Experimental Oncology, University Hospital München rechts der Isar; Technical University of Munich, Munich, Germany; Institute of Physiology and Immunology, Technical University of Munich, Freising-Weihenstephan, Germany. Electronic address: percy.knolle@tum.de.

Dirk Wohlleber (D)

Institute of Molecular Immunology and Experimental Oncology, University Hospital München rechts der Isar; Technical University of Munich, Munich, Germany.

Articles similaires

[Redispensing of expensive oral anticancer medicines: a practical application].

Lisanne N van Merendonk, Kübra Akgöl, Bastiaan Nuijen
1.00
Humans Antineoplastic Agents Administration, Oral Drug Costs Counterfeit Drugs

Smoking Cessation and Incident Cardiovascular Disease.

Jun Hwan Cho, Seung Yong Shin, Hoseob Kim et al.
1.00
Humans Male Smoking Cessation Cardiovascular Diseases Female
Humans United States Aged Cross-Sectional Studies Medicare Part C
1.00
Humans Yoga Low Back Pain Female Male

Classifications MeSH