Inhibition of virulence genes expression of phytopathogenic bacteria can be done by degrading the acyl-homoserine lactone (AHL) compounds using AHL-lactonase. In this study, the AHL-lactonase genes were cloned and expressed from Bacillus cereus INT1c and Bacillus thuringiensis SGT3g in Escherichia coli, in order to understand the characteristics and biocontrol mechanisms of their AHL-lactonase. Amplification using aiiA primers succeeded to get 800 bp DNA fragments of AHL-latonase genes having a complete open reading frame (ORF) and encoding 250 amino acids. AHL-lactonase genes of B. cereus INT1c and B. thuringiensis SGT3g were expressed in E. coli BL21 (DE3) plasmid with T7 lysozyme coding sequence (pLysS). AHL-lactonase of the isolates is classified as metallo-β-lactamase superfamily domain and the AHL-lactonase inhibited violacein production of Chromobacterium violaceum.
Key words: Acyl-homoserine lactone (AHL), lactonase, aiiA gene, cloning, Bacillus thuringiensis, Bacillus cereus.
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