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A quorum-sensing system using AHLs as the signal in many bacterial pathogens is a critical virulence regulator and an attractive target for anti-infective drugs. In this work, we identified a novel AHL lactonase, AidB, from a soil bacterial strain,Bosea sp. F3-2. The expression ofaidB reduced the production of AHL signals and QS-dependent virulence factors inPseudomonas aeruginosa andPectobacterium carotovorum . The homologs of AidB with AHL-degrading activities were found only in several genera belonging to theAlphaproteobacteria . Remarkably, AidB is a thermostable enzyme that retained its catalytic activity after treatment at 80°C for 30 min and exhibits reliable storage stability at both 4°C and room temperature. These properties might make it more suitable for practical application.

AidB, a Novel Thermostable N -Acylhomoserine Lactonase from the Bacterium Bosea sp