Evidence map›Paper›PMID 39885151›Full record

ArticleCell death & disease2025

Executioner caspases degrade essential mediators of pathogen-host interactions to inhibit growth of intracellular Listeria monocytogenes.

Marilyne Lavergne, Raffael Schaerer, Sara De Grandis, Safaa Bouheraoua, Oluwadamilola Adenuga, Tanja Muralt, Tiffany Schaerer, Léa Chèvre, Alessandro Failla, Patricia Matthey and 4 more

Abstract read
In one paragraph

Article in Cell death & disease, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

  1. Article
  2. A self-assembled and HTheranostics · 2025
    Article
  3. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

14 authors.

Marilyne LavergneFaculty of Science and Medicine, Department of Oncology, Microbiology and Immunology, Anatomy unit, University of Fribourg, CH-1700, Fribourg, Switzerland.
Raffael Schaerer *Faculty of Science and Medicine, Department of Oncology, Microbiology and Immunology, Anatomy unit, University of Fribourg, CH-1700, Fribourg, Switzerland.
Sara De Grandis *Faculty of Science and Medicine, Department of Oncology, Microbiology and Immunology, Anatomy unit, University of Fribourg, CH-1700, Fribourg, Switzerland.ORCID 0009-0000-9263-9298
Safaa Bouheraoua *Faculty of Science and Medicine, Department of Oncology, Microbiology and Immunology, Anatomy unit, University of Fribourg, CH-1700, Fribourg, Switzerland.
Oluwadamilola Adenuga *Faculty of Science and Medicine, Department of Oncology, Microbiology and Immunology, Anatomy unit, University of Fribourg, CH-1700, Fribourg, Switzerland.ORCID 0009-0008-6835-3327
Tanja MuraltFaculty of Science and Medicine, Department of Oncology, Microbiology and Immunology, Anatomy unit, University of Fribourg, CH-1700, Fribourg, Switzerland.
Tiffany SchaererFaculty of Science and Medicine, Department of Oncology, Microbiology and Immunology, Anatomy unit, University of Fribourg, CH-1700, Fribourg, Switzerland.ORCID 0009-0007-8008-9939
Léa ChèvreFaculty of Science and Medicine, Department of Oncology, Microbiology and Immunology, Anatomy unit, University of Fribourg, CH-1700, Fribourg, Switzerland.
Alessandro FaillaFaculty of Science and Medicine, Department of Oncology, Microbiology and Immunology, Anatomy unit, University of Fribourg, CH-1700, Fribourg, Switzerland.
Patricia MattheyFaculty of Science and Medicine, Department of Oncology, Microbiology and Immunology, Anatomy unit, University of Fribourg, CH-1700, Fribourg, Switzerland.
Michael StumpeFaculty of Science and Medicine, Department of Biology, Metabolomics and Proteomics Platform, University of Fribourg, CH-1700, Fribourg, Switzerland.
Dieter KresslerFaculty of Science and Medicine, Department of Biology, Metabolomics and Proteomics Platform, University of Fribourg, CH-1700, Fribourg, Switzerland.
Pierre-Yves MantelFaculty of Science and Medicine, Department of Oncology, Microbiology and Immunology, Anatomy unit, University of Fribourg, CH-1700, Fribourg, Switzerland.
Michael WalchFaculty of Science and Medicine, Department of Oncology, Microbiology and Immunology, Anatomy unit, University of Fribourg, CH-1700, Fribourg, Switzerland. michael.walch@unifr.ch.ORCID 0000-0001-7284-3291

Funding

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (Swiss National Science Foundation) 310030_1699Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (Swiss National Science Foundation) 31003A_182729
6 · The paper itself

Abstract

Cell death mediated by executioner caspases is essential during organ development and for organismal homeostasis. The mechanistic role of activated executioner caspases in antibacterial defense during infections with intracellular bacteria, such as Listeria monocytogenes, remains elusive. Cell death upon intracellular bacterial infections is considered altruistic to deprive the pathogens of their protective niche. To establish infections in a human host, Listeria monocytogenes deploy virulence mediators, including membranolytic listeriolysin O (LLO) and the invasion associated protein p60 (Iap), allowing phagosomal escape, intracellular replication and cell-to-cell spread. Here, by means of chemical and genetical modifications, we show that the executioner caspases-3 and -7 efficiently inhibit growth of intracellular Listeria monocytogenes in host cells. Comprehensive proteomics revealed multiple caspase-3 substrates in the Listeria secretome, including LLO, Iap and various other proteins crucially involved in pathogen-host interactions. Listeria secreting caspase-uncleavable LLO or Iap gained significant growth advantage in epithelial cells. With that, we uncovered an underappreciated defense barrier and a non-canonical role of executioner caspases to degrade virulence mediators, thus impairing intracellular Listeria growth.

Indexed as

Caspase 3Caspase 7CaspasesHost-Pathogen InteractionsListeria monocytogenesListeriosisBacterial ToxinsHeat-Shock ProteinsHemolysin ProteinsHumansBacterial ToxinsCaspase 3Caspase 7CaspasesHeat-Shock ProteinsHemolysin ProteinshlyA protein, Listeria monocytogenes

Identifiers

PMID39885151
PMCPMC11782612

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.