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The Role of AiiA, a Quorum-Quenching Enzyme from Bacillus thuringiensis, on the Rhizosphere Competence  

Park, Su-Jin (Systems Microbiology Research Center, KRIBB)
Park, Sun-Yang (Systems Microbiology Research Center, KRIBB)
Ryu, Choong-Min (Systems Microbiology Research Center, KRIBB)
Park, Seung-Hwan (Systems Microbiology Research Center, KRIBB)
Lee, Jung-Kee (Department of Life Science and Genetic Engineering, Paichai University)
Publication Information
Journal of Microbiology and Biotechnology / v.18, no.9, 2008 , pp. 1518-1521 More about this Journal
Abstract
Bacteria sense their population density and coordinate the expression of target genes, including virulence factors in Gram-negative bacteria, by the N-acylhomoserine lactones (AHLs)-dependent quorum sensing (QS) mechanism. In contrast, several soil bacteria are able to interfere with QS by enzymatic degradation of AHLs, referred to as quorum quenching. A potent AHL-degrading enzyme, AiiA, from Bacillus thuringiensis has been reported to effectively attenuate the virulence of bacteria by quorum quenching. However, little is known about the role of AiiA in B. thuringiensis itself. In the present study, an aiiA-defective mutant was generated to investigate the role of AHA in rhizosphere competence in the root system of pepper. The aiiA mutant showed no detectable AHL¬-egrading activity and was less effective for suppression of soft-rot symptom caused by Erwinia carotovora on the potato slice. On the pepper root, the survival rate of the aiiA mutant significantly decreased over time compared with that of wild type. Interestingly, viable cell count analysis revealed that the bacterial number and composition of E. carotovora were not different between treatments of wild type and the aiiA mutant. These results provide evidence that AHA can play an important role in rhizosphere competentce of B. thuringiensis and bacterial quorum quenching to Gram-negative bacteria without changing bacterial number or composition.
Keywords
Quorum sensing; quorum quenching; N-acylhomoserine lactone; AHL-lactonase; Bacillus thuringiensis;
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