Components of intestinal epithelial hypoxia activate the virulence circuitry of Pseudomonas

Am J Physiol Gastrointest Liver Physiol. 2005 May;288(5):G1048-54. doi: 10.1152/ajpgi.00241.2004. Epub 2004 Nov 18.

Abstract

We have previously shown that a lethal virulence trait in Pseudomonas aeruginosa, the PA-I lectin, is expressed by bacteria within the intestinal lumen of surgically stressed mice. The aim of this study was to determine whether intestinal epithelial hypoxia, a common response to surgical stress, could activate PA-I expression. A fusion construct was generated to express green fluorescent protein downstream of the PA-I gene, serving as a stable reporter strain for PA-I expression in P. aeruginosa. Polarized Caco-2 monolayers were exposed to ambient hypoxia (0.1-0.3% O2) for 1 h, with or without a recovery period of normoxia (21% O2) for 2 h, and then inoculated with P. aeruginosa containing the PA-I reporter construct. Hypoxic Caco-2 monolayers caused a significant increase in PA-I promoter activity relative to normoxic monolayers (165% at 1 h; P < 0.001). Similar activation of PA-I was also induced by cell-free apical, but not basal, media from hypoxic Caco-2 monolayers. PA-I promoter activation was preferentially enhanced in bacterial cells that physically interacted with hypoxic epithelia. We conclude that the virulence circuitry of P. aeruginosa is activated by both soluble and contact-mediated elements of the intestinal epithelium during hypoxia and normoxic recovery.

Publication types

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

MeSH terms

  • Adhesins, Bacterial / biosynthesis*
  • Adhesins, Bacterial / physiology
  • Caco-2 Cells
  • Cell Hypoxia / physiology
  • Genes, Reporter
  • Humans
  • Intestinal Mucosa / microbiology
  • Intestinal Mucosa / physiopathology*
  • Lectins / biosynthesis*
  • Lectins / physiology
  • Pseudomonas aeruginosa / genetics
  • Pseudomonas aeruginosa / pathogenicity*
  • Time Factors
  • Virulence

Substances

  • Adhesins, Bacterial
  • Lectins
  • adhesin, Pseudomonas