Luo Boyu, Wu Shanshan, Liu Wei, Zhang Dongdong, Liu Ruicun, Liu Tuoyu, Sun Zhi, Wei Ziqun, Liu Mingyu, Shi Zhiyuan, Huang Niu, Teng Yue
State Key Laboratory of Pathogen and Biosecurity, Academy of Military Medical Sciences, Beijing, 100071, China.
National Institute of Biological Sciences, No. 7 Science Park Road, Zhongguancun Life Science Park, Beijing, 102206, China.
Synth Syst Biotechnol. 2024 Oct 14;10(1):174-184. doi: 10.1016/j.synbio.2024.10.002. eCollection 2025.
YpsR, a pivotal regulatory protein in the quorum-sensing (QS) of (), is essential for molecular signaling, yet its molecular mechanisms remain poorly understood. Herein, this study systematically investigates the interactions between YpsR and acyl-homoserine lactones (AHLs), shedding light on the selective mechanism of YpsR to various AHL molecules. Using molecular docking and surface plasmon resonance (SPR) analysis, we confirmed YpsR's binding affinities, with the strongest observed for 3OC6-HSL, which notably inhibited growth. Additionally, we engineered a whole-cell biosensor based on YpsR-AHL interaction, which exhibited sensitivity to the signal molecule 3OC6-HSL produced by . Furthermore, key YpsR residues (S32, Y50, W54, D67) involved in AHL binding were identified and validated. Overall, this research elucidates the mechanisms of QS signal recognition in , providing valuable insights that support the development of diagnostic tools for detecting infections.
YpsR是（）群体感应（QS）中的一种关键调节蛋白，对分子信号传导至关重要，但其分子机制仍知之甚少。在此，本研究系统地研究了YpsR与酰基高丝氨酸内酯（AHLs）之间的相互作用，揭示了YpsR对各种AHL分子的选择性机制。通过分子对接和表面等离子体共振（SPR）分析，我们确定了YpsR的结合亲和力，其中对3OC6-HSL的亲和力最强，该物质显著抑制了生长。此外，我们基于YpsR-AHL相互作用构建了一种全细胞生物传感器，该传感器对由（）产生的信号分子3OC6-HSL具有敏感性。此外，还鉴定并验证了参与AHL结合的关键YpsR残基（S32、Y50、W54、D67）。总体而言，本研究阐明了（）中QS信号识别的机制，为开发检测（）感染的诊断工具提供了有价值的见解。
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