{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T00:05:14Z","timestamp":1790985914947,"version":"4.1.0"},"reference-count":54,"publisher":"Microbiology Society","issue":"9","funder":[{"name":"Graduate College 840"},{"name":"Ministry of Defence"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2011,9,1]]},"abstract":"<jats:p>\n                    <jats:italic>Burkholderia pseudomallei<\/jats:italic>\n                    is a facultative intracellular bacterial pathogen causing melioidosis, an often fatal infectious disease that is endemic in several tropical and subtropical areas around the world. We previously described a Ptk2 cell-based plaque assay screening system of\n                    <jats:italic>B. pseudomallei<\/jats:italic>\n                    transposon mutants that led to the identification of several novel virulence determinants. Using this approach we identified a mutant with reduced plaque formation in which the\n                    <jats:italic>BPSL0918<\/jats:italic>\n                    gene was disrupted.\n                    <jats:italic>BPSL0918<\/jats:italic>\n                    encodes a putative FK-506-binding protein (FKBP) representing a family of proteins that typically possess peptidyl-prolyl isomerase (PPIase) activity. A\n                    <jats:italic>B. pseudomallei<\/jats:italic>\n                    \u0394\n                    <jats:italic>BPSL0918<\/jats:italic>\n                    mutant showed a severely impaired ability to resist intracellular killing and to replicate within primary macrophages. Complementation of the mutant fully restored its ability to grow intracellularly. Moreover,\n                    <jats:italic>B. pseudomallei<\/jats:italic>\n                    \u0394\n                    <jats:italic>BPSL0918<\/jats:italic>\n                    was significantly attenuated in a murine model of infection. Structural modelling confirmed a modified FKBP fold of the\n                    <jats:italic>BPSL0918<\/jats:italic>\n                    -encoded protein but unlike virulence-associated FKBPs from other pathogenic bacteria, recombinant BPSL0918 protein did not possess PPIase activity\n                    <jats:italic>in vitro<\/jats:italic>\n                    . In accordance with this observation BPSL0918 exhibits several mutations in residues that have been proposed to mediate PPIase activity in other FKBPs. To our knowledge this\n                    <jats:italic>B. pseudomallei<\/jats:italic>\n                    FKBP represents the first example of this protein family which lacks PPIase activity but is important in intracellular infection of a bacterial pathogen.\n                  <\/jats:p>","DOI":"10.1099\/mic.0.049163-0","type":"journal-article","created":{"date-parts":[[2011,6,17]],"date-time":"2011-06-17T17:37:38Z","timestamp":1308332258000},"page":"2629-2638","source":"Crossref","is-referenced-by-count":26,"title":["A novel FK-506-binding-like protein that lacks peptidyl-prolyl isomerase activity is involved in intracellular infection and in vivo virulence of Burkholderia pseudomallei"],"prefix":"10.1099","volume":"157","author":[{"given":"Isobel H.","family":"Norville","sequence":"first","affiliation":[{"name":"Defence Science and Technology Laboratory, Porton Down, Salisbury SP4 0JQ, 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