{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T02:15:05Z","timestamp":1790734505790,"version":"4.1.0"},"reference-count":115,"publisher":"MDPI AG","issue":"2","license":[{"start":{"date-parts":[[2021,1,9]],"date-time":"2021-01-09T00:00:00Z","timestamp":1610150400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Myosins play a key role in many cellular processes such as cell migration, adhesion, intracellular trafficking and internalization processes, making them ideal targets for bacteria. Through selected examples, such as enteropathogenic E. coli (EPEC), Neisseria, Salmonella, Shigella, Listeria or Chlamydia, this review aims to illustrate how bacteria target and hijack host cell myosins in order to adhere to the cell, to enter the cell by triggering their internalization, to evade from the cytosolic autonomous cell defense, to promote the biogenesis of intracellular replicative niche, to disseminate in tissues by cell-to-cell spreading, to exit out the host cell, and also to evade from macrophage phagocytosis. It highlights the diversity and sophistication of the strategy evolved by bacteria to manipulate one of their privileged targets, the actin cytoskeleton.<\/jats:p>","DOI":"10.3390\/ijms22020615","type":"journal-article","created":{"date-parts":[[2021,1,10]],"date-time":"2021-01-10T19:55:56Z","timestamp":1610308556000},"page":"615","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Myosins, an Underestimated Player in the Infectious Cycle of Pathogenic Bacteria"],"prefix":"10.3390","volume":"22","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0736-3288","authenticated-orcid":false,"given":"Margaux","family":"Pillon","sequence":"first","affiliation":[{"name":"CIRI, Centre International de Recherche en Infectiologie, Legionella Pathogenesis Group, Universit\u00e9 de Lyon, 69007 Lyon, France"},{"name":"Institut National de la Sant\u00e9 et de la Recherche M\u00e9dicale (INSERM), U1111, 69007 Lyon, France"},{"name":"Ecole Normale Sup\u00e9rieure de Lyon, 69007 Lyon, France"},{"name":"Centre International de Recherche en Infectiologie, Universit\u00e9 Claude Bernard Lyon 1, 69007 Lyon, France"},{"name":"Centre National de la Recherche Scientifique, UMR5308, 69007 Lyon, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5848-4317","authenticated-orcid":false,"given":"Patricia","family":"Doublet","sequence":"additional","affiliation":[{"name":"CIRI, Centre International de Recherche en Infectiologie, Legionella Pathogenesis Group, Universit\u00e9 de Lyon, 69007 Lyon, France"},{"name":"Institut National de la Sant\u00e9 et de la Recherche M\u00e9dicale (INSERM), U1111, 69007 Lyon, France"},{"name":"Ecole Normale Sup\u00e9rieure de Lyon, 69007 Lyon, France"},{"name":"Centre International de Recherche en Infectiologie, Universit\u00e9 Claude Bernard Lyon 1, 69007 Lyon, France"},{"name":"Centre National de la Recherche Scientifique, UMR5308, 69007 Lyon, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,1,9]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"4617","DOI":"10.1021\/bi00801a004","article-title":"Mechanism of adenosine triphosphate hydrolysis by actomyosin","volume":"10","author":"Lymn","year":"1971","journal-title":"Biochemistry"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1126\/science.8316858","article-title":"Structure of the actin-myosin complex and its implications for muscle contraction","volume":"261","author":"Rayment","year":"1993","journal-title":"Science"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"13137","DOI":"10.1016\/S0021-9258(18)43018-9","article-title":"Reversible phosphorylation of smooth muscle myosin, heavy meromyosin, and platelet myosin","volume":"256","author":"Sellers","year":"1981","journal-title":"J. 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