School of Chemistry, Chemical Engineering, and Life Science, Wuhan University of Technology, Wuhan, China.
School of Energy and Power Engineering, Wuhan University of Technology, Wuhan, China.
Microbiologyopen. 2019 Aug;8(8):e00797. doi: 10.1002/mbo3.797. Epub 2019 Feb 14.
Magnetic immobilization of quorum sensing (QS) signal hydrolases provides a convenient solution for quenching QS process that is essential for bacterial biofilm formation and antimicrobial resistance. In the present study, a QS signal hydrolase, AiiA, was fused with a magnetic protein, MagR, and expressed in Escherichia coli. Magnetic immobilization of AiiA was achieved on Fe O -SiO iron beads and was confirmed via SDS-PAGE, zeta potential measurement, FTIR spectrometry, and SEM analysis. The magnetic immobilized AiiA exhibited activity in degrading the quorum sensing signal, C6-HSL. This study opens a new avenue to actively immobilize enzymes via magnetic interaction and quench quorum sensing.
群体感应(QS)信号水解酶的磁固定为淬灭 QS 过程提供了一种便利的解决方案,QS 过程对于细菌生物膜形成和抗菌药物耐药性至关重要。在本研究中,QS 信号水解酶 AiiA 与磁性蛋白 MagR 融合,并在大肠杆菌中表达。AiiA 通过 Fe₃O₄-SiO₂铁珠实现了磁性固定,并通过 SDS-PAGE、ζ电位测量、FTIR 光谱和 SEM 分析进行了确认。磁性固定的 AiiA 表现出降解群体感应信号 C6-HSL 的活性。这项研究为通过磁相互作用主动固定酶和淬灭群体感应开辟了新途径。