Listeriolysin S: A bacteriocin from Listeria monocytogenes that induces membrane permeabilization in a contact-dependent manner

Jazmín Meza-Torres; Mickaël Lelek; Juan Quereda; Martin Sachse; Giulia Manina; Dmitry Ershov; Jean-Yves Tinevez; Lilliana Radoshevich; Claire Maudet; Thibault Chaze; Quentin Giai Gianetto; Mariette Matondo; Marc Lecuit; Isabelle Martin-Verstraete; Christophe Zimmer; Hélène Bierne; Olivier Dussurget; Pascale Cossart; Javier Pizarro-Cerdá

doi:10.1073/pnas.2108155118

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Listeriolysin S: A bacteriocin from Listeria monocytogenes that induces membrane permeabilization in a contact-dependent manner

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Listeriolysin S: A bacteriocin from Listeria monocytogenes that induces membrane permeabilization in a contact-dependent manner

Jazmín Meza-Torres, Mickaël Lelek, Juan Quereda, Martin Sachse, Giulia Manina, Dmitry Ershov, Jean-Yves Tinevez, Lilliana Radoshevich, Claire Maudet, Thibault Chaze, …

Proceedings of the National Academy of Sciences - PNAS, Vol.118(40), p.e2108155118

10/05/2021

DOI: 10.1073/pnas.2108155118

PMCID: PMC8501752

PMID: 34599102

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Abstract

Significance Listeria monocytogenes ( Lm ) is a bacterial pathogen that causes listeriosis, a foodborne disease characterized by gastroenteritis, meningitis, bacteremia, and abortions in pregnant women. The most severe human listeriosis outbreaks are associated with a subset of Lm hypervirulent clones that encode the bacteriocin Listeriolysin S (LLS), which modifies the gut microbiota and allows efficient Lm gut colonization and invasion of deeper organs. Our present work identifies the killing mechanism displayed by LLS to outcompete gut commensal bacteria, demonstrating that it induces membrane permeabilization and membrane depolarization of target bacteria. Moreover, we show that LLS is a thiazole/oxazole–modified microcin that displays a contact-dependent inhibition mechanism.

Adenosine Triphosphate

Bacteriocins

Bacteriology

Cell Membrane

Cytoplasm

Hemolysin Proteins

Life Sciences

Listeria monocytogenes

Microbiology and Parasitology

Details

Title: Subtitle: Listeriolysin S: A bacteriocin from Listeria monocytogenes that induces membrane permeabilization in a contact-dependent manner
Creators: Jazmín Meza-Torres - Sorbonne Paris Cité
Mickaël Lelek - Institut Pasteur
Juan Quereda - Universidad Cardenal Herrera CEU
Martin Sachse - Institut Pasteur
Giulia Manina - Institut Pasteur
Dmitry Ershov - Institut Pasteur
Jean-Yves Tinevez - Institut Pasteur
Lilliana Radoshevich - Roy J. and Lucille A. Carver College of Medicine
Claire Maudet - Institut Pasteur
Thibault Chaze - Institut Pasteur
Quentin Giai Gianetto - Spectrométrie de Masse pour la Biologie – Mass Spectrometry for Biology
Mariette Matondo - Institut Pasteur
Marc Lecuit - Sorbonne Paris Cité
Isabelle Martin-Verstraete - Centre National pour la Recherche Scientifique et Technique (CNRST)
Christophe Zimmer - Institut Pasteur
Hélène Bierne - Epigenetics and Cellular Microbiology Laboratory, Université Paris-Saclay, Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement, AgroParisTech, 78352 Jouy-en-Josas, France.
Olivier Dussurget - Institut Pasteur
Pascale Cossart - Institut Pasteur
Javier Pizarro-Cerdá - Institut Pasteur
Resource Type: Journal article
Publication Details: Proceedings of the National Academy of Sciences - PNAS, Vol.118(40), p.e2108155118
DOI: 10.1073/pnas.2108155118
PMID: 34599102
PMCID: PMC8501752
NLM abbreviation: Proc Natl Acad Sci U S A
ISSN: 0027-8424
eISSN: 1091-6490
Publisher: National Academy of Sciences
Grant note: name: Institut Carnot Pasteur Microbes et Santé, award: PasteurInnov Grant LLS-Bact; name: Region Ile-de-France, award: DIM-MALINF; DOI: 10.13039/501100002915, name: Fondation pour la Recherche Médicale, award: FDT201904008152; name: Ramon y Cajal, award: RYC-2018-024985-I; name: LabEX IBEID, award: ANR LBX-62 IBEID
Language: English
Date published: 10/05/2021
Academic Unit: Molecular Physiology and Biophysics; Microbiology and Immunology
Record Identifier: 9984297437202771

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