A burkholderia pseudomallei macrophage infectivity potentiator-like protein has rapamycin-inhibitable peptidylprolyl isomerase activity and pleiotropic effects on virulence

I.H. H. Norville, N.J. J. Harmer, S.V. V. Harding, G. Fischer, K.E. E. Keith, K.A. A. Brown, Mitali Sarkar-Tyson, R.W. W. Titball

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22 Citations (Scopus)

Abstract

Macrophage infectivity potentiators (Mips) are a group of virulence factors encoded by pathogenic bacteria such as Legionella, Chlamydia, and Neisseria species. Mips are part of the FK506-binding protein (FKBP) family, whose members typically exhibit peptidylprolyl cis-trans 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 Burkholderia pseudomallei. Recombinant BPSS1823 protein has rapamycin-inhibitable PPIase activity, indicating that it is a functional FKBP. A mutant strain generated by deletion of BPSS1823 in B. pseudomallei exhibited a reduced ability to survive within cells and significant attenuation in vivo, suggesting that BPSS1823 is important for B. pseudomallei virulence. In addition, pleiotropic effects were observed with a reduction in virulence mechanisms, including resistance to host killing mechanisms, swarming motility, and protease production. © 2011, American Society for Microbiology.
Original languageEnglish
Pages (from-to)4299-4307
Number of pages9
JournalInfection and Immunity
Volume79
Issue number11
DOIs
Publication statusPublished - 2011
Externally publishedYes

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