{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,20]],"date-time":"2026-06-20T09:59:26Z","timestamp":1781949566228,"version":"3.54.5"},"reference-count":27,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2018,11,19]],"date-time":"2018-11-19T00:00:00Z","timestamp":1542585600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100000038","name":"Natural Sciences and Engineering Research Council of Canada","doi-asserted-by":"publisher","award":["355316"],"award-info":[{"award-number":["355316"]}],"id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["anatomypubs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The Anatomical Record"],"published-print":{"date-parts":[[2018,12]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p><jats:italic>Salmonella enterica<\/jats:italic> serovar Typhimurium (<jats:italic>S<\/jats:italic>. Typhimurium), enteropathogenic <jats:styled-content style=\"fixed-case\"><jats:italic>Escherichia coli<\/jats:italic><\/jats:styled-content> (EPEC) and enterohemorrhagic <jats:styled-content style=\"fixed-case\"><jats:italic>E. coli<\/jats:italic><\/jats:styled-content> (EHEC) commandeer the actin cytoskeleton of their host cells as a crucial step in their infectious processes. These pathogens depend on the injection of their own effectors directly into target host cells in order to usurp cellular signaling pathways that lead to morphological actin rearrangements in those cells. Here we show that the PPIase Cyclophilin A (CypA) is a novel component of <jats:italic>S<\/jats:italic>. Typhimurium\u2010induced membrane ruffles and functions to restrict bacterial invasion levels, as in cells depleted of CypA, bacterial loads increase. We also demonstrate that CypA requires the EPEC effector Tir as well as pedestal formation for its recruitment to bacterial attachment sites and that its presence at pedestals also holds during EHEC infections. Finally, we demonstrate that CypA is found at lamellipodia; actin\u2010rich structures at the leading edge of motile cells. Our findings further establish CypA as a component of dynamic actin\u2010rich structures formed during bacterial infections and within cells in general. Anat Rec, 301:2086\u20132094, 2018. \u00a9 2018 Wiley Periodicals, Inc.<\/jats:p>","DOI":"10.1002\/ar.23957","type":"journal-article","created":{"date-parts":[[2018,10,12]],"date-time":"2018-10-12T11:07:05Z","timestamp":1539342425000},"page":"2086-2094","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["Cyclophilin A Controls <i>Salmonella<\/i> Internalization Levels and is Present at <scp><i>E. coli<\/i><\/scp> Actin\u2010Rich Pedestals"],"prefix":"10.1002","volume":"301","author":[{"given":"Aaron S.","family":"Dhanda","sequence":"first","affiliation":[{"name":"Department of Biological Sciences Faculty of Science, Simon Fraser University  Burnaby British Columbia Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kiera E.","family":"Warren","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences Faculty of Science, Simon Fraser University  Burnaby British Columbia Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert H.","family":"Chiu","sequence":"additional","affiliation":[{"name":"Dental and Craniofacial Research Institute and School of Dentistry University of California  Los Angeles California"},{"name":"Surgical Oncology &amp; Jonsson Comprehensive Cancer Center University of California  Los Angeles California"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8852-1593","authenticated-orcid":false,"given":"Julian A.","family":"Guttman","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences Faculty of Science, Simon Fraser University  Burnaby British Columbia Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2018,11,19]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1128\/JB.182.8.2341-2344.2000"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1462-5822.2006.00762.x"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.chom.2007.02.001"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1007\/s11010-008-9896-0"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.2001.02617.x"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1038\/364639a0"},{"key":"e_1_2_7_8_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.1997.mmi525.x"},{"key":"e_1_2_7_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)81442-7"},{"key":"e_1_2_7_10_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.92.17.7996"},{"key":"e_1_2_7_11_1","doi-asserted-by":"publisher","DOI":"10.1038\/14087"},{"key":"e_1_2_7_12_1","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.1999.01265.x"},{"key":"e_1_2_7_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)80437-7"},{"key":"e_1_2_7_14_1","doi-asserted-by":"publisher","DOI":"10.1038\/329268a0"},{"key":"e_1_2_7_15_1","doi-asserted-by":"publisher","DOI":"10.1021\/acs.jproteome.5b00074"},{"key":"e_1_2_7_16_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1088433"},{"key":"e_1_2_7_17_1","doi-asserted-by":"publisher","DOI":"10.1016\/S1097-2765(04)00053-X"},{"key":"e_1_2_7_18_1","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.41.3.1340-1351.1983"},{"key":"e_1_2_7_19_1","doi-asserted-by":"publisher","DOI":"10.1002\/j.1460-2075.1992.tb05438.x"},{"key":"e_1_2_7_20_1","first-page":"399","article-title":"Distribution 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