Bdellovibrio bacteriovorus inhibits Staphylococcus aureus biofilm formation and invasion into human epithelial cells

Sci Rep. 2014 Jan 22:4:3811. doi: 10.1038/srep03811.

Abstract

Bdellovibrio bacteriovorus HD100 is a predatory bacterium that attacks many Gram-negative human pathogens. A serious drawback of this strain, however, is its ineffectiveness against Gram-positive strains, such as the human pathogen Staphylococcus aureus. Here we demonstrate that the extracellular proteases produced by a host-independent B. bacteriovorus (HIB) effectively degrade/inhibit the formation of S. aureus biofilms and reduce its virulence. A 10% addition of HIB supernatant caused a 75% or greater reduction in S. aureus biofilm formation as well as 75% dispersal of pre-formed biofilms. LC-MS-MS analyses identified various B. bacteriovorus proteases within the supernatant, including the serine proteases Bd2269 and Bd2321. Tests with AEBSF confirmed that serine proteases were active in the supernatant and that they impacted S. aureus biofilm formation. The supernatant also possessed a slight DNAse activity. Furthermore, treatment of planktonic S. aureus with the supernatant diminished its ability to invade MCF-10a epithelial cells by 5-fold but did not affect the MCF-10a viability. In conclusion, this study illustrates the hitherto unknown ability of B. bacteriovorus to disperse Gram-positive pathogenic biofilms and mitigate their virulence.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bdellovibrio / physiology*
  • Biofilms / drug effects
  • Biofilms / growth & development*
  • Breast / metabolism
  • Cell Proliferation
  • Cells, Cultured
  • Chromatography, Liquid
  • Epithelial Cells / drug effects
  • Epithelial Cells / metabolism
  • Epithelial Cells / microbiology*
  • Female
  • Humans
  • Protease Inhibitors / pharmacology
  • Serine Endopeptidases / metabolism*
  • Staphylococcal Infections / microbiology
  • Staphylococcal Infections / prevention & control*
  • Staphylococcus aureus / pathogenicity*
  • Tandem Mass Spectrometry
  • Virulence*

Substances

  • Protease Inhibitors
  • Serine Endopeptidases