LsrB-based and temperature-dependent identification of bacterial AI-2 receptor

文献类型： 外文期刊

第一作者： Zhang, Yuxi

作者： Zhang, Yuxi;Jing, Yawei;Zuo, Jiakun;Hu, Jiangang;Lv, Xiaolong;Chen, Zhaoguo;Mi, Rongsheng;Huang, Yan;Yu, Shengqing;Han, Xiangan;Zhang, Yuxi;Qi, Kezong

作者机构：

关键词： Escherichia coli BL21;LuxS mutant;LsrB;AI-2 receptor

期刊名称：AMB EXPRESS （ 影响因子：3.298； 五年影响因子：3.427 ）

ISSN： 2191-0855

年卷期： 2017 年 7 卷

页码：

收录情况： SCI

摘要： The luxS gene is required for autoinducer-2 (AI-2) synthesis in many bacterial species. AI-2 is taken up by a specific receptor to regulate multiple bacterial activities. However, the lack of methods to identify AI-2 receptors has impeded investigations into the roles of AI-2. Here, a luxS mutant of Escherichia coli strain BL21 (DE3) was constructed (named BL21 Delta luxS), and the recombinant LsrB protein of Salmonella enterica was expressed in BL21 Delta luxS and BL21 cells, which were named LsrB (BL21 Delta luxS) and LsrB (BL21), respectively. The results of the activity of recombinant LsrB binding showed that LsrB (BL21) bound to endogenous AI-2 (produced from BL21 strain), while LsrB (BL21 Delta luxS) did not (as BL21 Delta luxS cannot produce AI-2). However, the results of recombinant LsrB binding showed that LsrB (BL21 Delta luxS) can bind exogenous AI-2, which was released from LsrB (BL21 Delta luxS) at 55 degrees C for 10 min, while LsrB (BL21) could not bind exogenous AI-2 (due to binding of endogenous AI-2 before). Furthermore, analysis of the thermal stability of AI-2 showed that that AI-2 activity was relatively high at incubation temperatures below 65 degrees C. These findings will be beneficial for screening of new AI-2 receptors in different bacterial species.

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