Rapid degradation of N-3-oxo-acylhomoserine lactones by a Bacillus cereus isolate from Malaysian rainforest soil

Antonie Van Leeuwenhoek. 2010 Oct;98(3):299-305. doi: 10.1007/s10482-010-9438-0. Epub 2010 Apr 8.

Abstract

A bacterial strain, KM1S, was isolated from a Malaysian rainforest soil sample by using a defined enrichment medium that specifically facilitates selection of quorum quenching bacteria. KM1S was clustered closely to Bacillus cereus by 16S ribosomal DNA sequence analysis. It degraded N-3-oxo-hexanoyl homoserine lactone and N-3-oxo-octanoyl homoserine lactone in vitro rapidly at 4.98 and 6.56 microg AHL h(-1) per 10(9) CFU/ml, respectively, as determined by the Rapid Resolution Liquid Chromatography. The aiiA homologue, encoding an autoinducer inactivation enzyme catalyzing the degradation of N-acylhomoserine lactones, of KM1S was amplified and cloned. Sequence analysis indicated the presence of the motif (106)HXDH-59 amino acids-H(169)-21 amino acids-D(191) for N-acylhomoserine lactone lactonases.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 4-Butyrolactone / analogs & derivatives
  • 4-Butyrolactone / metabolism
  • Acyl-Butyrolactones / metabolism*
  • Amino Acid Sequence
  • Bacillus cereus / genetics
  • Bacillus cereus / isolation & purification
  • Bacillus cereus / metabolism*
  • Bacterial Proteins / metabolism
  • Carboxylic Ester Hydrolases / biosynthesis*
  • Chromobacterium / metabolism
  • Cloning, Molecular
  • DNA, Bacterial
  • Escherichia coli / genetics
  • Genes, Bacterial
  • Gram-Negative Bacteria
  • Malaysia
  • Molecular Sequence Data
  • Quorum Sensing
  • Sequence Analysis, DNA
  • Soil Microbiology*
  • Trees

Substances

  • Acyl-Butyrolactones
  • Bacterial Proteins
  • DNA, Bacterial
  • homoserine lactone
  • Carboxylic Ester Hydrolases
  • N-acyl homoserine lactonase
  • 4-Butyrolactone

Associated data

  • GENBANK/FJ827748
  • GENBANK/FJ827749