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Once in the intestines, these microbes generate various actin\u2010rich structures to attach, invade, or move within the host intestinal epithelial cells. Although an assortment of actin\u2010associated proteins has been identified to varying degrees at these structures, the localization of many actin stabilizing proteins have yet to be analyzed. Here, we examined the recruitment of the actin\u2010associated proteins, calponin 1 and 2 at EPEC pedestals, <jats:styled-content style=\"fixed-case\"><jats:italic>L. monocytogenes<\/jats:italic><\/jats:styled-content> actin clouds, comet tails and listeriopods, and <jats:italic>S<\/jats:italic>. Typhimurium membrane ruffles. In other systems, calponins are known to bind to and stabilize actin filaments. In EPEC pedestals, calponin 1 was recruited uniformly throughout the structures while calponin 2 was enriched at the apical tip. During <jats:styled-content style=\"fixed-case\"><jats:italic>L. monocytogenes<\/jats:italic><\/jats:styled-content> infections, calponin 1 was found through all the actin\u2010rich structures generated by the bacteria, while calponin 2 was only present within actin\u2010rich structures formed by <jats:styled-content style=\"fixed-case\"><jats:italic>L. monocytogenes<\/jats:italic><\/jats:styled-content> near the host cell membrane. Finally, both calponins were found within <jats:italic>S<\/jats:italic>. Typhimurium\u2010generated membrane ruffles. Taken together, we have shown that although calponin 1 is recruited to actin\u2010rich structures formed by the three bacteria, calponin 2 is specifically recruited to only membrane\u2010bound actin\u2010rich structures formed by the bacteria. Thus, our findings suggest that calponin 2 is a novel marker for membrane\u2010bound actin structures formed by pathogenic bacteria. Anat Rec, 301:2103\u20132111, 2018. \u00a9 2018 Wiley Periodicals, Inc.<\/jats:p>","DOI":"10.1002\/ar.23956","type":"journal-article","created":{"date-parts":[[2018,10,12]],"date-time":"2018-10-12T12:30:39Z","timestamp":1539347439000},"page":"2103-2111","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Calponins Are Recruited to Actin\u2010Rich Structures Generated by Pathogenic <scp><i>Escherichia coli<\/i><\/scp>, <i>Listeria<\/i>, and <i>Salmonella<\/i>"],"prefix":"10.1002","volume":"301","author":[{"given":"Michael Dominic","family":"Chua","sequence":"first","affiliation":[{"name":"Department of Biological Sciences Simon Fraser University  Burnaby British Columbia Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Brittany Dominique","family":"Walker","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences Simon Fraser University  Burnaby British Columbia 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