Open AccessListeriolysin S: A bacteriocin from Listeria monocytogenes that induces membrane permeabilization in a contact-dependent manner
Author(s) -
Jazmín Meza-Torres,
Mickaël Lelek,
Juan J. Quereda,
Martin Sachse,
Giulia Manina,
Dmitry Ershov,
Jean-Yves Tinévez,
Lilliana Radoshevich,
Claire Maudet,
Thibault Chaze,
Quentin Giai Gianetto,
Mariette Matondo,
Marc Lecuit,
Isabelle MartinVerstraete,
Christophe Zimmer,
Hélène Bierne,
Olivier Dussurget,
Pascale Cossart,
Javier PizarroCerdá
Publication year - 2021
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2108155118
Subject(s) - listeria monocytogenes , bacteria , listeriolysin o , bacteriocin , microbiology and biotechnology , bacterial cell structure , chemistry , biology , listeria , genetics
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 ofLm hypervirulent clones that encode the bacteriocin Listeriolysin S (LLS), which modifies the gut microbiota and allows efficientLm 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.