CFTR and pseudomonas infections in cystic fibrosis

Front Biosci. 2001 Aug 1;6:D890-7. doi: 10.2741/tatterso.


Pseudomonas aeruginosa is a significant threat to human health as it is frequently recalcitrant to conventional antibacterial therapy. This ubiquitous gram-negative bacterium is notorious for its nutritional and ecological flexibility and its resistance to both antibiotic treatments and sanitary measures. These properties contribute to its prominence as a leading source of opportunistic nosocomial (hospital acquired) and a less appreciated, but significant cause of community acquired infections. P. aeruginosa remains a considerable problem for patients with burns, neutropenic individuals, and cystic fibrosis patients (CF). In this review, we will address the current issues in P. aeruginosa infections in CF. A major emphasis will be placed on the factors predisposing CF patients to colonization with P. aeruginosa.

Publication types

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

MeSH terms

  • Animals
  • Bacterial Adhesion
  • Biofilms / growth & development
  • Cystic Fibrosis / complications*
  • Cystic Fibrosis / metabolism
  • Cystic Fibrosis / microbiology
  • Cystic Fibrosis Transmembrane Conductance Regulator / genetics*
  • Disease Models, Animal
  • Humans
  • Inflammation / immunology
  • Mice
  • Nitric Oxide Synthase / biosynthesis
  • Nitric Oxide Synthase Type II
  • Pseudomonas Infections / complications
  • Pseudomonas Infections / metabolism
  • Pseudomonas Infections / microbiology*
  • Pseudomonas aeruginosa / pathogenicity*
  • Pseudomonas aeruginosa / physiology
  • Respiratory Mucosa / enzymology
  • Respiratory Mucosa / microbiology
  • Respiratory Tract Infections / complications
  • Respiratory Tract Infections / metabolism
  • Respiratory Tract Infections / microbiology*
  • Sialyltransferases / metabolism


  • CFTR protein, human
  • Cystic Fibrosis Transmembrane Conductance Regulator
  • NOS2 protein, human
  • Nitric Oxide Synthase
  • Nitric Oxide Synthase Type II
  • Nos2 protein, mouse
  • Sialyltransferases