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

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

Edité par CCSD ; National Academy of Sciences -

International audience. 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.

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