Oct 13, 2019

AidB, a novel thermostable N -acylhomoserine lactonase from the bacterium Bosea sp

Applied and Environmental Microbiology
Jun-Wei ZhangLi-Qun Zhang


Many Gram-negative bacteria employ N-acylhomoserine lactones (AHLs) as quorum sensing (QS) signal molecules to regulate virulence expression in a density-dependent manner. Quorum quenching (QQ) via enzymatic inactivation of AHLs is a promising strategy to reduce bacterial infections and drug resistance. Herein, a thermostable AHL lactonase (AidB), which could degrade different AHLs, with or without a substitution of carbonyl or hydroxyl at the C-3 position, was identified from the soil bacterium Bosea sp. F3-2. Ultra-high performance liquid chromatography analysis demonstrated that AidB is an AHL lactonase that hydrolyzes the ester bond of the homoserine lactone ring. AidB was thermostable in the range 30 to 80 °C and showed maximum activity after pre-incubating at 60 °C for 30 min. The optimum temperature of AidB was 60 °C, and the enzyme could be stably stored in ddH2O at 4 °C or room temperature. AidB homologs were only found in Rhizobiales and Rhodospirillales of the α-Proteobacteria AidBAt from Agrobacterium and AidBRm from Rhizobium (amino acid identities of 50.6% and 52.8% to AidB, respectively) also showed thermostable AHL degradation activity. When introduced into bacteria, plasmid-expressed AidB attenuated pyocyanin p...Continue Reading

  • References50
  • Citations1


  • References50
  • Citations1


Mentioned in this Paper

Positioning Attribute
Operating Room
Molecular Probe Techniques
Hydroxyl group
AidB protein, E coli
Gram-Negative Bacteria
Pharmacologic Substance
Pseudomonas aeruginosa
High Pressure Liquid Chromatography Procedure

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