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

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...

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Bibliographic Details
Published in:Antonie van Leeuwenhoek 2010-10, Vol.98 (3), p.299-305
Main Authors: Chan, Kok-Gan, Wong, Cheng-Siang, Yin, Wai-Fong, Sam, Choon-Kook, Koh, Chong-Lek
Format: Article
Language:English
Subjects:
4-Butyrolactone - analogs & derivatives
4-Butyrolactone - metabolism
Acyl-Butyrolactones - metabolism
Amino Acid Sequence
Amino acids
Bacillus cereus
Bacillus cereus - genetics
Bacillus cereus - isolation & purification
Bacillus cereus - metabolism
Bacteria
Bacterial Proteins - metabolism
Bacteriology
Biochemistry
Biological and medical sciences
Carboxylic Ester Hydrolases - biosynthesis
Chromobacterium - metabolism
Cloning, Molecular
DNA, Bacterial
Escherichia coli - genetics
Fundamental and applied biological sciences. Psychology
Genes, Bacterial
Gram-Negative Bacteria
Inactivation
KG medium
Liquid chromatography
Malaysia
Microbiology
Miscellaneous
Molecular Sequence Data
N-acylhomoserine lactone
Quorum quenching
Quorum Sensing
Rainforest soil
Rainforests
Sequence Analysis, DNA
Soil Microbiology
Soil sciences
Trees
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Summary: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 μg AHL h⁻¹ per 10⁹ 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 ₁₀₆HXDH-59 amino acids-H₁₆₉-21 amino acids-D₁₉₁ for N-acylhomoserine lactone lactonases.
ISSN:0003-6072
1572-9699
DOI:10.1007/s10482-010-9438-0