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- W2979707555 abstract "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 of aidB reduced the production of AHL signals and QS-dependent virulence factors in Pseudomonas aeruginosa and Pectobacterium carotovorum . The homologs of AidB with AHL-degrading activities were found only in several genera belonging to the Alphaproteobacteria . 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." @default.
- W2979707555 created "2019-10-18" @default.
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- W2979707555 date "2019-12-01" @default.
- W2979707555 modified "2023-10-15" @default.
- W2979707555 title "AidB, a Novel Thermostable <i>N</i> -Acylhomoserine Lactonase from the Bacterium <i>Bosea</i> sp" @default.
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- W2979707555 doi "https://doi.org/10.1128/aem.02065-19" @default.
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