Characterization the Function of Quorum-quenching N-Acylhomoserine Lactonase AiiS from Shinella sp. 37-1

doi:10.16409/j.cnki.2095-039x.2021.04.007

Abstract

Abstract: The expression of multiple virulence factors is regulated by quorum sensing (QS) in many phytopathogenic bacteria. Quorum quenching (QQ), which influences the function of QS by either disruption of QS signals or the process of signal production and perception, is a promising strategy for attenuating the pathogenicity of these bacteria. In this study, we isolated and screened rhizobacteria with QQ activity. One candidate 37-1 was obtained and identified as a Shinella sp. strain based on 16S rDNA gene analysis. Bioinformatics and genetic analyses indicated that aiiS gene (autoinducer inactivation gene from Shinella sp.) was responsible for the degradation of N-acylhomoserine lactone (AHL). High-performance liquid chromatography/tandem mass spectrometry (HPLC-MS/MS) analysis further demonstrated that AiiS was an AHL lactonase that hydrolyzed the ester bond of the homoserine lactone ring. In addition, the production of AHLs, the activity of pectate lyases, and the virulence on host plants were significantly attenuated when overexpression of aiiS gene in Pectobacterium carotovorum subsp. carotovorum Z3-3. These results suggested that AiiS was an AHL lactonase, and pathogenic bacteria harboring aiiS gene could interfere efficiently with quorum-sensing-regulated functions, suggesting that AiiS could be a potential biocontrol agent for developing quorum-quenching procedures.

Key words: quorum-sensing system, quorum quenching, N-acylhomoserine lactones, lactonase

CLC Number:

S476

RAO Ronghua, ZHANG Junwei, WU Xiaogang. Characterization the Function of Quorum-quenching N-Acylhomoserine Lactonase AiiS from Shinella sp. 37-1[J]. Chinese Journal of Biological Control, 2021, 37(4): 826-836.

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