{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T08:26:33Z","timestamp":1791275193517,"version":"4.1.0"},"reference-count":64,"publisher":"American Society for Microbiology","issue":"12","license":[{"start":{"date-parts":[[2010,12,1]],"date-time":"2010-12-01T00:00:00Z","timestamp":1291161600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2010,12]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            <jats:italic>Listeria monocytogenes<\/jats:italic>\n            interaction with the intestinal epithelium is a key step in the infection process. We demonstrated that\n            <jats:italic>Listeria<\/jats:italic>\n            adhesion protein (LAP) promotes adhesion to intestinal epithelial cells and facilitates extraintestinal dissemination\n            <jats:italic>in vivo<\/jats:italic>\n            . The LAP receptor is a stress response protein, Hsp60, but the precise role for the LAP-Hsp60 interaction during\n            <jats:italic>Listeria<\/jats:italic>\n            infection is unknown. Here we investigated the influence of physiological stressors and\n            <jats:italic>Listeria<\/jats:italic>\n            infection on host Hsp60 expression and LAP-mediated bacterial adhesion, invasion, and transepithelial translocation in an enterocyte-like Caco-2 cell model. Stressors such as heat (41\u00b0C), tumor necrosis factor alpha (TNF-\u03b1) (100 U), and\n            <jats:italic>L. monocytogenes<\/jats:italic>\n            infection (10\n            <jats:sup>4<\/jats:sup>\n            to 10\n            <jats:sup>6<\/jats:sup>\n            CFU\/ml) significantly (\n            <jats:italic>P<\/jats:italic>\n            &lt; 0.05) increased plasma membrane and intracellular Hsp60 levels in Caco-2 cells and consequently enhanced LAP-mediated\n            <jats:italic>L. monocytogenes<\/jats:italic>\n            adhesion but not invasion of Caco-2 cells. In transepithelial translocation experiments, the wild type (WT) exhibited 2.7-fold more translocation through Caco-2 monolayers than a\n            <jats:italic>lap<\/jats:italic>\n            mutant, suggesting that LAP is involved in transepithelial translocation, potentially via a paracellular route. Short hairpin RNA (shRNA) suppression of Hsp60 in Caco-2 cells reduced WT adhesion and translocation 4.5- and 3-fold, respectively, while adhesion remained unchanged for the\n            <jats:italic>lap<\/jats:italic>\n            mutant. Conversely, overexpression of Hsp60 in Caco-2 cells enhanced WT adhesion and transepithelial translocation, but not those of the\n            <jats:italic>lap<\/jats:italic>\n            mutant. Furthermore, initial infection with a low dosage (10\n            <jats:sup>6<\/jats:sup>\n            CFU\/ml) of\n            <jats:italic>L. monocytogenes<\/jats:italic>\n            increased plasma membrane and intracellular expression of Hsp60 significantly, which rendered Caco-2 cells more susceptible to subsequent LAP-mediated adhesion and translocation. These data provide insight into the role of LAP as a virulence factor during intestinal epithelial infection and pose new questions regarding the dynamics between the host stress response and pathogen infection.\n          <\/jats:p>","DOI":"10.1128\/iai.00516-10","type":"journal-article","created":{"date-parts":[[2010,9,28]],"date-time":"2010-09-28T04:24:12Z","timestamp":1285647852000},"page":"5062-5073","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":106,"title":["<i>Listeria monocytogenes<\/i>\n            Uses Listeria Adhesion Protein (LAP) To Promote Bacterial Transepithelial Translocation and Induces Expression of LAP Receptor Hsp60"],"prefix":"10.1128","volume":"78","author":[{"given":"Kristin M.","family":"Burkholder","sequence":"first","affiliation":[{"name":"Molecular Food Microbiology Laboratory, Department of Food Science"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arun K.","family":"Bhunia","sequence":"additional","affiliation":[{"name":"Molecular Food Microbiology Laboratory, Department of Food Science"},{"name":"Department of Comparative Pathobiology, Purdue University, West Lafayette, Indiana 47907"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.65.1.78-88.1997"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0906112107"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.69.7.4657-4660.2001"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.67.8.4191-4200.1999"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1006\/bbrc.2000.3663"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.micinf.2009.05.006"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2003.03945.x"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1038\/sj.emboj.7600750"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M206525200"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.1993.tb01211.x"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.174.2.568-574.1992"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.micpath.2006.08.003"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.ymgme.2005.04.003"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0962-8924(02)00006-5"},{"key":"e_1_3_2_16_2","doi-asserted-by":"publisher","DOI":"10.1097\/00004630-199405000-00002"},{"key":"e_1_3_2_17_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.71.2.682-689.2003"},{"key":"e_1_3_2_18_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2004.04138.x"},{"key":"e_1_3_2_19_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.67.7.3512-3517.1999"},{"key":"e_1_3_2_20_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.68.11.6321-6328.2000"},{"key":"e_1_3_2_21_2","doi-asserted-by":"publisher","DOI":"10.1093\/intimm\/4.3.305"},{"key":"e_1_3_2_22_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrmicro2171"},{"key":"e_1_3_2_23_2","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.67.3.1262-1267.2001"},{"key":"e_1_3_2_24_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2672.2005.02559.x"},{"key":"e_1_3_2_25_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.64.4.1299-1308.1996"},{"key":"e_1_3_2_26_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M705904200"},{"key":"e_1_3_2_27_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.01479-06"},{"key":"e_1_3_2_28_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0016-5085(89)80072-1"},{"key":"e_1_3_2_29_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1432-1033.2002.03317.x"},{"key":"e_1_3_2_30_2","doi-asserted-by":"publisher","DOI":"10.1099\/mic.0.036509-0"},{"key":"e_1_3_2_31_2","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.69.6.3640-3645.2003"},{"key":"e_1_3_2_32_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00430-002-0150-1"},{"key":"e_1_3_2_33_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6968.2006.00140.x"},{"key":"e_1_3_2_34_2","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.71.11.7528-7530.2005"},{"key":"e_1_3_2_35_2","first-page":"55","volume":"2","year":"2001","unstructured":"Konkel, M., M. 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