Abstract
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 Fe3O4‐SiO2 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.
Highlights
Quorum sensing (QS) is a bacterial type of cell–cell communication by which bacteria regulates the expression of specific genes in‐ volved in biofilm formation, adhesion, antibiotic synthesis, virulence, swarming, bioluminescence, mating, and tissue damage (Bassler, 2002; Davies, Parsek, Pearson, Iglewski, & Costerton, 1998)
It contributes to the antimicrobial resistance that leads to the failure of anti‐infection treatment after implant surgery since biofilm retards the diffusion of antibiotics, and prevents patho‐ genic bacteria from attacking of immune cells
A magnetic protein, MagR, as a fusion tag was placed at C‐terminus of a quorum sensing signal hydrolase, AiiA
Summary
Quorum sensing (QS) is a bacterial type of cell–cell communication by which bacteria regulates the expression of specific genes in‐ volved in biofilm formation, adhesion, antibiotic synthesis, virulence, swarming, bioluminescence, mating, and tissue damage (Bassler, 2002; Davies, Parsek, Pearson, Iglewski, & Costerton, 1998). Inhibition of QS is often required on specific sur‐ faces such as implant surface This can be achieved by immo‐ bilizing enzymes to degrade or modify QS signals in a specific area. Enzyme can be immobilized with chemical or physical means by modifying enzymes or supports/carriers to allow specific interactions between each other, by using bi‐ or. The use of magnetic protein MagR as fusion tag has been recently reported for actively immobilizing GFP and lipase (Jiang, Zhang, Wang, Zhang, & Liu, 2017). The enzymatic activity of IB@[AiiA‐MagR] in degrading AHLs was analyzed
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