Deinococcus radiodurans can interfere with quorum sensing by producing an AHL-acylase and an AHL-lactonase

FEMS Microbiol Lett. 2014 Jul;356(1):62-70. doi: 10.1111/1574-6968.12479. Epub 2014 Jun 26.

Abstract

Bacterial communication via the secretion of small diffusible compounds allows microorganisms to regulate gene expression in a coordinated manner. As many virulence traits are regulated in this fashion, disruption of chemical communication has been proposed as novel antimicrobial therapy. Quorum-quenching enzymes have been a promising discovery in this field as they interfere with the communication of Gram-negative bacteria. AHL-lactonases and AHL-acylases have been described in a variety of bacterial strains; however, usually only one of these two groups of enzymes has been described in a single species. We report here the presence of a member of each group of enzymes in the extremophile bacterium Deinococcus radiodurans. Co-occurrence of both enzymes in a single species increases the chance of inactivating foreign AHL signals under different conditions. We demonstrate that both enzymes are able to degrade the quorum-sensing molecules of various pathogens subsequently affecting virulence gene expression. These studies add the quorum-quenching enzymes of D. radiodurans to the list of potent quorum-quenchers and highlight the idea that quorum quenching could have evolved in some bacteria as a strategy to gain a competitive advantage by altering gene expression in other species.

Keywords: acyl homoserine lactone; acylase; extremophile; lactonase; quorum sensing.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyl-Butyrolactones / metabolism
  • Amidohydrolases / chemistry
  • Amidohydrolases / physiology*
  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / physiology*
  • Caenorhabditis elegans / microbiology
  • Carboxylic Ester Hydrolases / chemistry
  • Carboxylic Ester Hydrolases / physiology*
  • Deinococcus / enzymology*
  • Molecular Sequence Data
  • Pseudomonas aeruginosa / physiology
  • Quorum Sensing*

Substances

  • Acyl-Butyrolactones
  • Bacterial Proteins
  • Carboxylic Ester Hydrolases
  • N-acyl homoserine lactonase
  • Amidohydrolases