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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\u2013modified microcin that displays a contact-dependent inhibition mechanism.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2108155118","type":"journal-article","created":{"date-parts":[[2021,10,1]],"date-time":"2021-10-01T17:35:36Z","timestamp":1633109736000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":43,"title":["Listeriolysin S: A bacteriocin from\n                    <i>Listeria monocytogenes<\/i>\n                    that induces membrane permeabilization in a contact-dependent manner"],"prefix":"10.1073","volume":"118","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2603-8544","authenticated-orcid":false,"given":"Jazm\u00edn","family":"Meza-Torres","sequence":"first","affiliation":[{"name":"Yersinia Research Unit, Microbiology Department, Institut Pasteur, 75015 Paris, France;"},{"name":"Bacteria-Cell Interactions Unit, Cell Biology and Infection Department, 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