The Multifunctional Protein YdiV Represses P Fimbria-Mediated Adherence in Uropathogenic Escherichia coli

• DOI: 10.1128/jb.02254-12
• Publication Date: 2013-05-11T04:33:03Z
• Authors: R. R. Spurbeck; C. J. Alteri; S. D. Himpsl; H. L. T. Mobley
• Keywords: Derepression

YdiV, a degenerate EAL domain protein, represses motility by interacting with FlhD to abolish FlhDC interaction DNA. Here, we demonstrate that deletion of ydiV dysregulates coordinate control and adherence increasing Escherichia coli CFT073 bladder epithelial cell line specifically production P fimbriae. Interestingly, only one the two fimbrial operons, pap_2, present in genome E. was upregulated. This derepression pap_2 operon is abolished following either cya or crp, demonstrating cyclic AMP (cAMP)-dependent activation operon. However, absence YdiV does not affect gene expression loss SdiA mutant operon, suggesting acts response cAMP levels. Deletion increases fliA, CFT073, regulates same mechanism as described previously for commensal strains. Furthermore, analysis site-directed mutations found putative Mg2+-binding residues four conserved (E29 Q219) were involved regulation FliC production, while c-di-GMP-binding (D156 D165) affected motility. None appeared adherence. Therefore, propose model which EAL, utilizes different domains regulate through cells cAMP-dependent effects on promoter.