Journal
EMBO JOURNAL
Volume 20, Issue 17, Pages 4854-4862Publisher
OXFORD UNIV PRESS
DOI: 10.1093/emboj/20.17.4854
Keywords
adherence; coordination; fimbriae; flagella; motility
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Funding
- NIDDK NIH HHS [R01 DK047920] Funding Source: Medline
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Proteus mirabilis is a common uropathogen in patients with long-term catheterization or with structural or functional abnormalities in the urinary tract. The mannose-resistant, Proteus-like (MR/P) fimbriae and flagellum are among virulence factors of P. mirabilis that contribute to its colonization in a murine model of ascending urinary tract infection. mrpJ, the last of nine genes of the mrp operon, encodes a 107 amino acid protein that contains a putative helix-turn-helix domain. Using transcriptional lacZ fusions integrated into the chromosome and mutagenesis studies, we demonstrate that MrpJ represses transcription of the flagellar regulon and thus reduces flagella synthesis when MR/P fimbriae are produced. The repression of flagella synthesis by MrpJ is confirmed by electron microscopy. However, a gel mobility shift assay indicates that MrpJ does not bind directly to the regulatory region of the flhDC operon. The isogenic mrpJ null mutant of wild-type P. mirabilis strain HI4320 is attenuated in the murine model. Our data also indicate that PapX encoded by a pap (pyelonephritis-associated pilus) operon of uropathogenic Escherichia coli is a functional homolog of MrpJ.
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