{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T18:20:12Z","timestamp":1790706012496,"version":"4.1.0"},"update-to":[{"DOI":"10.1371\/journal.ppat.1009932","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2021,9,21]],"date-time":"2021-09-21T00:00:00Z","timestamp":1632182400000}}],"reference-count":55,"publisher":"Public Library of Science (PLoS)","issue":"9","license":[{"start":{"date-parts":[[2021,9,9]],"date-time":"2021-09-09T00:00:00Z","timestamp":1631145600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["R01AI081724"],"award-info":[{"award-number":["R01AI081724"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["F32AI147549"],"award-info":[{"award-number":["F32AI147549"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["T32AI007061"],"award-info":[{"award-number":["T32AI007061"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["K22AI137296"],"award-info":[{"award-number":["K22AI137296"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["F32AI114162"],"award-info":[{"award-number":["F32AI114162"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Executive Committee on Research, Massachusetts General Hospital"},{"DOI":"10.13039\/100008601","name":"Charles A. King Trust","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100008601","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>\n                    Many bacterial pathogens require a type 3 secretion system (T3SS) to establish a niche. Host contact activates bacterial T3SS assembly of a translocon pore in the host plasma membrane. Following pore formation, the T3SS docks onto the translocon pore. Docking establishes a continuous passage that enables the translocation of virulence proteins, effectors, into the host cytosol. Here we investigate the contribution of actin polymerization to T3SS-mediated translocation. Using the T3SS model organism\n                    <jats:italic>Shigella flexneri<\/jats:italic>\n                    , we show that actin polymerization is required for assembling the translocon pore in an open conformation, thereby enabling effector translocation. Opening of the pore channel is associated with a conformational change to the pore, which is dependent upon actin polymerization and a coiled-coil domain in the pore protein IpaC. Analysis of an IpaC mutant that is defective in ruffle formation shows that actin polymerization-dependent pore opening is distinct from the previously described actin polymerization-dependent ruffles that are required for bacterial internalization. Moreover, actin polymerization is not required for other pore functions, including docking or pore protein insertion into the plasma membrane. Thus, activation of the T3SS is a multilayered process in which host signals are sensed by the translocon pore leading to the activation of effector translocation.\n                  <\/jats:p>","DOI":"10.1371\/journal.ppat.1009932","type":"journal-article","created":{"date-parts":[[2021,9,9]],"date-time":"2021-09-09T14:21:19Z","timestamp":1631197279000},"page":"e1009932","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":16,"title":["The type 3 secretion system requires actin polymerization to open translocon pores"],"prefix":"10.1371","volume":"17","author":[{"given":"Brian C.","family":"Russo","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3615-9596","authenticated-orcid":true,"given":"Jeffrey K.","family":"Duncan-Lowey","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9302-0400","authenticated-orcid":true,"given":"Poyin","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4266-9733","authenticated-orcid":true,"given":"Marcia B.","family":"Goldberg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2021,9,9]]},"reference":[{"key":"ppat.1009932.ref001","first-page":"326","article-title":"Type III secretion: more systems than you think","volume":"20","author":"P Troisfontaines","year":"2005","journal-title":"Physiology (Bethesda)."},{"issue":"12","key":"ppat.1009932.ref002","doi-asserted-by":"crossref","DOI":"10.3390\/microorganisms8121933","article-title":"The T3SS of Shigella: Expression, Structure, Function, and Role in Vacuole Escape","volume":"8","author":"W Bajunaid","year":"2020","journal-title":"Microorganisms."},{"key":"ppat.1009932.ref003","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1146\/annurev-micro-092412-155725","article-title":"Bacterial type III secretion systems: specialized nanomachines for protein delivery into target cells","volume":"68","author":"JE Galan","year":"2014","journal-title":"Annual review of microbiology"},{"issue":"7","key":"ppat.1009932.ref004","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1515\/bc.2010.079","article-title":"The type III secretion injectisome, a complex nanomachine for intracellular \u2019toxin\u2019 delivery","volume":"391","author":"GR Cornelis","year":"2010","journal-title":"Biol Chem"},{"issue":"11","key":"ppat.1009932.ref005","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1038\/nrmicro1526","article-title":"The type III secretion injectisome","volume":"4","author":"GR Cornelis","year":"2006","journal-title":"Nat Rev Microbiol"},{"issue":"2","key":"ppat.1009932.ref006","doi-asserted-by":"crossref","DOI":"10.3390\/microorganisms9020451","article-title":"The Shigella Type III Secretion System: An Overview from Top to Bottom","volume":"9","author":"M Muthuramalingam","year":"2021","journal-title":"Microorganisms"},{"issue":"12","key":"ppat.1009932.ref007","doi-asserted-by":"crossref","first-page":"e1007380","DOI":"10.1371\/journal.ppat.1007380","article-title":"Principles of intracellular bacterial pathogen spread from cell to cell","volume":"14","author":"E Weddle","year":"2018","journal-title":"PLoS pathogens"},{"issue":"1","key":"ppat.1009932.ref008","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/j.mib.2008.12.002","article-title":"Shigella type III secretion effectors: how, where, when, for what purposes?","volume":"12","author":"C. 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