Bacterial quorum sensing quenching activity of Lysobacter leucyl aminopeptidase acts by interacting with autoinducer synthase

文献类型： 外文期刊

第一作者： Liao, Jinxing

作者： Liao, Jinxing;Shen, Danyu;Lin, Long;Qian, Guoliang;Chen, Hongjun;Jin, Yajie;Li, Tao;Chou, Shan-Ho;Yu, Xiao-Quan

作者机构：

关键词： Quorum sensing; AHL; Quorum quenching; AHL synthase; Autoinducer; Lysobacter; Aminopeptidase

期刊名称：COMPUTATIONAL AND STRUCTURAL BIOTECHNOLOGY JOURNAL （ 影响因子：6.155； 五年影响因子：6.836 ）

ISSN： 2001-0370

年卷期： 2021 年 19 卷

页码：

收录情况： SCI

摘要： Acyl-homoserine lactone (AHL) is the most studied autoinducer in gram-negative bacteria controlling infections of various pathogens. Quenching of AHL signaling by inhibiting AHL synthesis or AHL-receptor binding via small molecular chemicals or enzymatically degrading AHL is commonly used to block bacterial infections. Here, we describe a new quorum-quenching strategy that directly "acquires" bacterial genes/proteins through a defined platform. We artificially expressed a typical AHL synthase gene pcoI from the biocontrol Pseudomonas fluorescens 2P24 in the antifungal bacterium Lysobacter enzymogenes OH11 lacking AHL production. This step led to the discovery of multiple PcoI interacting protein candidates from L. enzymogenes. The individual expression of these candidate genes in 2P24 led to the identification of Le0959, which encodes leucyl aminopeptidase, an effective protein that inhibits AHL synthesis in 2P24. Therefore, we define Le0959 as LqqP (Lysobacter quorum-quenching protein). The expression of pcoI in E. coli could produce AHL, and the introduction of lqqP into E. coli expressing pcoI could prevent the production of AHL. LqqP directly binds to PcoI, and this protein-protein binding reduced the abundance of free PcoI (capable of AHL synthesis) in vivo, thereby blocking PcoI-dependent AHL production. Overall, this study highlights the discovery of LqqP in quenching AHL quorum sensing by binding to AHL synthase via developing a previously-uncharacterized screening technique for bacterial quorum quenching. (C) 2021 The Author(s). Published by Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology.

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