{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,23]],"date-time":"2026-04-23T02:33:58Z","timestamp":1776911638108,"version":"3.51.2"},"reference-count":45,"publisher":"American Society for Microbiology","issue":"11","license":[{"start":{"date-parts":[[2011,11,1]],"date-time":"2011-11-01T00:00:00Z","timestamp":1320105600000},"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":[[2011,11]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Macrophage infectivity potentiators (Mips) are a group of virulence factors encoded by pathogenic bacteria such as\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Legionella<\/jats:named-content>\n                    ,\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Chlamydia<\/jats:named-content>\n                    , and\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Neisseria<\/jats:named-content>\n                    species. Mips are part of the FK506-binding protein (FKBP) family, whose members typically exhibit peptidylprolyl\n                    <jats:italic>cis-trans<\/jats:italic>\n                    isomerase (PPIase) activity which is inhibitable by the immunosuppressants FK506 and rapamycin. Here we describe the identification and characterization of BPSS1823, a Mip-like protein in the intracellular pathogen\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Burkholderia pseudomallei<\/jats:named-content>\n                    . Recombinant BPSS1823 protein has rapamycin-inhibitable PPIase activity, indicating that it is a functional FKBP. A mutant strain generated by deletion of\n                    <jats:italic>BPSS1823<\/jats:italic>\n                    in\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. pseudomallei<\/jats:named-content>\n                    exhibited a reduced ability to survive within cells and significant attenuation\n                    <jats:italic>in vivo<\/jats:italic>\n                    , suggesting that BPSS1823 is important for\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. pseudomallei<\/jats:named-content>\n                    virulence. In addition, pleiotropic effects were observed with a reduction in virulence mechanisms, including resistance to host killing mechanisms, swarming motility, and protease production.\n                  <\/jats:p>","DOI":"10.1128\/iai.00134-11","type":"journal-article","created":{"date-parts":[[2011,8,22]],"date-time":"2011-08-22T20:22:36Z","timestamp":1314044556000},"page":"4299-4307","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":41,"title":["A Burkholderia pseudomallei Macrophage Infectivity Potentiator-Like Protein Has Rapamycin-Inhibitable Peptidylprolyl Isomerase Activity and Pleiotropic Effects on Virulence"],"prefix":"10.1128","volume":"79","author":[{"given":"Isobel H.","family":"Norville","sequence":"first","affiliation":[{"name":"Defence Science and Technology Laboratory, Porton Down SP4 0JQ, United Kingdom"},{"name":"College of Life and Environmental Sciences, University of Exeter, Exeter EX4 4QD, United Kingdom"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nicholas J.","family":"Harmer","sequence":"additional","affiliation":[{"name":"College of Life and Environmental Sciences, University of Exeter, Exeter EX4 4QD, United Kingdom"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sarah V.","family":"Harding","sequence":"additional","affiliation":[{"name":"Defence Science and Technology Laboratory, Porton Down SP4 0JQ, United Kingdom"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gunter","family":"Fischer","sequence":"additional","affiliation":[{"name":"Max Plank Research Unit for Enzymology of Protein Folding, Halle, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Karen E.","family":"Keith","sequence":"additional","affiliation":[{"name":"Centre for Molecular Microbiology and Infection, Imperial College London, London SW7 2AZ, United Kingdom"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Katherine A.","family":"Brown","sequence":"additional","affiliation":[{"name":"Centre for Molecular Microbiology and Infection, Imperial College London, London SW7 2AZ, United Kingdom"},{"name":"Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mitali","family":"Sarkar-Tyson","sequence":"additional","affiliation":[{"name":"Defence Science and Technology Laboratory, Porton Down SP4 0JQ, United Kingdom"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Richard W.","family":"Titball","sequence":"additional","affiliation":[{"name":"College of Life and Environmental Sciences, University of Exeter, Exeter EX4 4QD, United Kingdom"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6976.2009.00189.x"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/aem.44.3.561-569.1982"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1186\/1472-6807-8-17"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/CMR.18.2.383-416.2005"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.71.4.1622-1629.2003"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0035-9203(08)70031-2"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.57.4.1255-1262.1989"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1093\/infdis\/162.1.121"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.89.11.5188"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.3201\/eid0912.020750"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.274.40.28436"},{"key":"e_1_3_2_13_2","first-page":"5.6","article-title":"Comparative protein structure modeling using Modeller","volume":"5","author":"Eswar N.","year":"2006","unstructured":"EswarN.. 2006. 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