A recA-LexA-dependent pathway mediates ciprofloxacin-induced fibronectin binding in Staphylococcus aureus

J Biol Chem. 2004 Mar 5;279(10):9064-71. doi: 10.1074/jbc.M309836200. Epub 2003 Dec 29.

Abstract

Subinhibitory concentrations of ciprofloxacin (CPX) raise the fibronectin-mediated attachment of fluoroquinolone-resistant Staphylococcus aureus by selectively inducing fnbB coding for one of two fibronectin-binding proteins: FnBPB. To identify candidate regulatory pathway(s) linking drug exposure to up-regulation of fnbB, we disrupted the global response regulators agr, sarA, and recA in the highly quinolone-resistant strain RA1. Whereas agr and sarA mutants of RA1 exposed to CPX still displayed increased adhesion to fibronectin, the CPX-triggered response was abolished in the uvs-568 recA mutant, but was restored following complementation with wild type recA. Steady-state levels of recA and fnbB, but not fnbA, mRNA were co-coordinately increased >3-fold in CPX-exposed strain RA1. Electrophoretic mobility shift assays revealed specific binding of purified S. aureus SOS-repressor LexA to recA and fnbB, but not to fnbA or rpoB promoters. DNase I footprint analysis showed LexA binding overlapping the core promoter elements in fnbB. We conclude that activation of recA and derepression of lexA-regulated genes by CPX may represent a response to drug-induced damage that results in a novel induction of a virulence factor leading to increased bacterial tissue adherence.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Anti-Infective Agents / pharmacology
  • Bacterial Adhesion / drug effects
  • Bacterial Proteins / metabolism*
  • Base Sequence
  • Ciprofloxacin / pharmacology
  • Fibronectins / genetics
  • Fibronectins / metabolism*
  • Molecular Sequence Data
  • Promoter Regions, Genetic
  • Protein Binding
  • Rec A Recombinases / genetics
  • Rec A Recombinases / metabolism*
  • Serine Endopeptidases / metabolism*
  • Staphylococcus aureus / metabolism*

Substances

  • Anti-Infective Agents
  • Bacterial Proteins
  • Fibronectins
  • LexA protein, Bacteria
  • Ciprofloxacin
  • Rec A Recombinases
  • Serine Endopeptidases