{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T14:04:31Z","timestamp":1791295471044,"version":"4.1.0"},"reference-count":39,"publisher":"National Academy of Sciences","issue":"7","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2010,2,16]]},"abstract":"<jats:p>\n                    The human pathogens enteropathogenic (EPEC) and enterohemorrhagic\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    and the related mouse pathogen\n                    <jats:italic>Citrobacter rodentium<\/jats:italic>\n                    subvert a variety of host cell signaling pathways via their plethora of type III secreted effectors, including triggering of an early apoptotic response. EPEC-infected cells do not develop late apoptotic symptoms, however. In this study we demonstrate that the NleH family effectors, homologs of the\n                    <jats:italic>Shigella<\/jats:italic>\n                    effector kinase OspG, blocks apoptosis. During EPEC infection, NleH effectors inhibit elevation of cytosolic Ca\n                    <jats:sup>2+<\/jats:sup>\n                    concentrations, nuclear condensation, caspase-3 activation, and membrane blebbing and promote cell survival. NleH1 alone is sufficient to prevent procaspase-3 cleavage induced by the proapoptotic compounds staurosporine, brefeldin A, and tunicamycin. Using\n                    <jats:italic>C. rodentium<\/jats:italic>\n                    , we found that NleH inhibits procaspase-3 cleavage at the bacterial attachment sites in vivo. A yeast two-hybrid screen identified the endoplasmic reticulum six-transmembrane protein Bax inhibitor-1 (BI-1) as an NleH-interacting partner. We mapped the NleH-binding site to the N-terminal 40 amino acids of BI-1. Knockdown of BI-1 resulted in the loss of NleH\u2019s antiapoptotic activity. These results indicate that NleH effectors are inhibitors of apoptosis that may act through BI-1 to carry out their cytoprotective function.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0911609106","type":"journal-article","created":{"date-parts":[[2010,1,26]],"date-time":"2010-01-26T23:49:26Z","timestamp":1264549766000},"page":"3129-3134","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":131,"title":["NleH effectors interact with Bax inhibitor-1 to block apoptosis during enteropathogenic\n                    <i>Escherichia coli<\/i>\n                    infection"],"prefix":"10.1073","volume":"107","author":[{"given":"Cordula","family":"Hemrajani","sequence":"first","affiliation":[{"name":"Centre for Molecular Microbiology and Infection, Division of Cell and Molecular Biology, Imperial College London, London SW7 2AZ, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cedric N.","family":"Berger","sequence":"additional","affiliation":[{"name":"Centre for Molecular Microbiology and Infection, Division of Cell and Molecular Biology, Imperial College London, London SW7 2AZ, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Keith S.","family":"Robinson","sequence":"additional","affiliation":[{"name":"Centre for Molecular Microbiology and Infection, Division of Cell and Molecular Biology, Imperial College London, London SW7 2AZ, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Olivier","family":"March\u00e8s","sequence":"additional","affiliation":[{"name":"Centre for Molecular Microbiology and Infection, Division of Cell and Molecular Biology, Imperial College London, London SW7 2AZ, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aurelie","family":"Mousnier","sequence":"additional","affiliation":[{"name":"Centre for Molecular Microbiology and Infection, Division of Cell and Molecular Biology, Imperial College London, London SW7 2AZ, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gad","family":"Frankel","sequence":"additional","affiliation":[{"name":"Centre for Molecular Microbiology and Infection, Division of Cell and Molecular Biology, Imperial College London, London SW7 2AZ, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2010,1,26]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.1128\/CMR.11.1.142"},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1462-5822.2005.00625.x"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.55.1.69-77.1987"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.1998.01144.x"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.73.5.2573-2585.2005"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.01238-08"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0604891103"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0400326101"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0504466102"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.00742-08"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1462-5822.2004.00421.x"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1172\/JCI11138"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1462-5822.2006.00820.x"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.67.5.2575-2584.1999"},{"key":"e_1_3_3_15_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1462-5822.2001.00103.x"},{"key":"e_1_3_3_16_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1056-8719(97)00033-6"},{"key":"e_1_3_3_17_2","doi-asserted-by":"publisher","DOI":"10.1080\/01926230701320337"},{"key":"e_1_3_3_18_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrc883"},{"key":"e_1_3_3_19_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)80434-1"},{"key":"e_1_3_3_20_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrm1150"},{"key":"e_1_3_3_21_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj3260001"},{"key":"e_1_3_3_22_2","first-page":"2893","article-title":"Induction of apoptosis by staurosporine involves the inhibition of expression of the major cell cycle proteins at the G(2)\/m checkpoint accompanied by alterations in Erk and Akt kinase activities","volume":"29","author":"Antonsson A","year":"2009","unstructured":"A Antonsson, JL Persson, Induction of apoptosis by staurosporine involves the inhibition of expression of the major cell cycle proteins at the G(2)\/m checkpoint accompanied by alterations in Erk and Akt kinase activities. 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