Pseudomonas Aeruginosa Extracellular Products Inhibit Staphylococcal Growth, and Disrupt Established Biofilms Produced by Staphylococcus Epidermidis

Microbiology. 2009 Jul;155(Pt 7):2148-2156. doi: 10.1099/mic.0.028001-0. Epub 2009 Apr 23.

Abstract

Multiple bacterial species often coexist as communities, and compete for environmental resources. Here, we describe how an opportunistic pathogen, Pseudomonas aeruginosa, uses extracellular products to interact with the nosocomial pathogen Staphylococcus epidermidis. S. epidermidis biofilms and planktonic cultures were challenged with P. aeruginosa supernatant cultures overnight. Results indicated that quorum-sensing-controlled factors from P. aeruginosa supernatant inhibited S. epidermidis growth in planktonic cultures. We also found that P. aeruginosa extracellular products, mainly polysaccharides, disrupted established S. epidermidis biofilms. Cellulase-treated P. aeruginosa supernatant, and supernatant from pelA, pslF and pelApslBCD mutants, which are deficient in polysaccharide biosynthesis, diminished the disruption of S. epidermidis biofilms. In contrast, S. epidermidis supernatant in overnight cultures had no effect on established P. aeruginosa biofilms and planktonic growth. These findings reveal that P. aeruginosa extracellular products are important microbial competition factors that overcome competition with S. epidermidis, and the results may provide clues for the development of a novel strategy for controlling S. epidermidis biofilms.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biofilms*
  • Carboxylic Ester Hydrolases / metabolism
  • Colony Count, Microbial
  • Polysaccharide-Lyases / deficiency
  • Polysaccharides, Bacterial / biosynthesis
  • Pseudomonas aeruginosa / metabolism*
  • Quinolones / metabolism
  • Quorum Sensing
  • Staphylococcus epidermidis / physiology*

Substances

  • 2-heptyl-3-hydroxy-4-quinolone
  • Polysaccharides, Bacterial
  • Quinolones
  • Carboxylic Ester Hydrolases
  • N-acyl homoserine lactonase
  • Polysaccharide-Lyases
  • pectate lyase