文献类型：期刊文献

英文题名：Differential binding of LuxR in response to temperature gauges switches virulence gene expression in Vibrio alginolyticus

作者：Cai, Jingxiao[1];Hao, Yuan[1];Xu, Rongjing[5];Zhang, Yuanxing[2,3];Ma, Yue[1,3,4];Zhang, Yibei[1,3];Wang, Qiyao[1,3,4]

机构：[1]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]Southern Marine Sci & Engn Guangdong Lab Zhuhai, Zhuhai 519000, Peoples R China;[3]Shanghai Engn Res Ctr Maricultured Anim Vaccines, Shanghai 200237, Peoples R China;[4]Shanghai Collaborat Innovat Ctr Biomfg, 130 Meilong Rd, Shanghai 200237, Peoples R China;[5]Yantai Tianyuan Aquat Co Ltd, Yantai, Shandong, Peoples R China

年份：2022

卷号：263

外文期刊名：MICROBIOLOGICAL RESEARCH

收录：;EI(收录号：20223012416056);WOS:【SCI-EXPANDED(收录号:WOS:000842991200001)】；

基金：This work was supported by grants from National Key Research and Development Program of China (2022YFE0101200) ; National Natural Science Foundation of China (31772891 to WQY, 31772893 to MY) ; China Agriculture Research System of MOF and MARA (CARS-47) and Postdoctoral Science Foundation of China (2021M701206 to ZYB) .

语种：英文

外文关键词：Bacterial pathogen; ChIP-seq; LuxR; Vibrio alginolyticus; Virulence

摘要：Vibrio pathogens must cope with temperature changes for proper thermo-adaptation and virulence gene expression. LuxR is a quorum-sensing (QS) master regulator of vibrios, playing roles in response to temperature alteration. However, the molecular mechanisms how LuxR is involved in adapting to different temperatures in bacteria have not been precisely elucidated. In this study, using chromatin immunoprecipitation and nucleotide sequencing (ChIP-seq), we identified 272 and 22 enriched loci harboring LuxR-binding peaks at ambient tem-perature (30 C) and heat shock (42 C) in the Vibrio alginolyticus genome, respectively. Analysis with the MEME (multiple EM for motif elicitation) algorithm indicated that the binding motifs of LuxR varied from temperatures. Three novel binding regions (the promoter of orf00292, orf00397 and fadD) of LuxR were identified and verified that the rising temperature causes the decreasing binding affinity of LuxR to these promoters. Meanwhile, the expression of orf00292, orf00397 and fadD were regulated by LuxR. Moreover, the weak binding of LuxR to the promoter of extracellular protease (Asp) was attributed to the attenuated Asp expression at thermal stress conditions. Taken together, our study demonstrated distinct binding characteristics of LuxR in response to temperature changes, thus highlighting LuxR as a thermo-sensor to switch and control virulence gene expression in V. alginolyticus.