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Magnetic immobilization of a quorum sensing signal hydrolase, AiiA
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 exp...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6692522/ https://www.ncbi.nlm.nih.gov/pubmed/30767416 http://dx.doi.org/10.1002/mbo3.797 |
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author | Wang, Lin Xu, Haixing Liu, Zewen Sun, Taolei Yuan, Chengqing Yang, Ying Guo, Junhui Xie, Hao |
author_facet | Wang, Lin Xu, Haixing Liu, Zewen Sun, Taolei Yuan, Chengqing Yang, Ying Guo, Junhui Xie, Hao |
author_sort | Wang, Lin |
collection | PubMed |
description | 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(3)O(4)‐SiO(2) 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. |
format | Online Article Text |
id | pubmed-6692522 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-66925222019-08-16 Magnetic immobilization of a quorum sensing signal hydrolase, AiiA Wang, Lin Xu, Haixing Liu, Zewen Sun, Taolei Yuan, Chengqing Yang, Ying Guo, Junhui Xie, Hao Microbiologyopen Original Articles 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(3)O(4)‐SiO(2) 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. John Wiley and Sons Inc. 2019-02-14 /pmc/articles/PMC6692522/ /pubmed/30767416 http://dx.doi.org/10.1002/mbo3.797 Text en © 2019 The Authors. MicrobiologyOpen published by John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Articles Wang, Lin Xu, Haixing Liu, Zewen Sun, Taolei Yuan, Chengqing Yang, Ying Guo, Junhui Xie, Hao Magnetic immobilization of a quorum sensing signal hydrolase, AiiA |
title | Magnetic immobilization of a quorum sensing signal hydrolase, AiiA |
title_full | Magnetic immobilization of a quorum sensing signal hydrolase, AiiA |
title_fullStr | Magnetic immobilization of a quorum sensing signal hydrolase, AiiA |
title_full_unstemmed | Magnetic immobilization of a quorum sensing signal hydrolase, AiiA |
title_short | Magnetic immobilization of a quorum sensing signal hydrolase, AiiA |
title_sort | magnetic immobilization of a quorum sensing signal hydrolase, aiia |
topic | Original Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6692522/ https://www.ncbi.nlm.nih.gov/pubmed/30767416 http://dx.doi.org/10.1002/mbo3.797 |
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