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A myxobacterial GH19 lysozyme with bacteriolytic activity on both Gram-positive and negative phytopathogens
Myxobacteria, as predatory bacteria, have good application potential in the biocontrol of pathogenic microorganisms. Extracellular enzymes are thought to play an important role in their predation and also provide resources for discovering new antibacterial molecules. We previously isolated a myxobac...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Springer Berlin Heidelberg
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9098779/ https://www.ncbi.nlm.nih.gov/pubmed/35551524 http://dx.doi.org/10.1186/s13568-022-01393-y |
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author | Li, Yueqiu Zhou, Xiaoli Zhang, Xianjiao Xu, Zhiqiang Dong, Honghong Yu, Guohui Cheng, Ping Yao, Qing Zhu, Honghui |
author_facet | Li, Yueqiu Zhou, Xiaoli Zhang, Xianjiao Xu, Zhiqiang Dong, Honghong Yu, Guohui Cheng, Ping Yao, Qing Zhu, Honghui |
author_sort | Li, Yueqiu |
collection | PubMed |
description | Myxobacteria, as predatory bacteria, have good application potential in the biocontrol of pathogenic microorganisms. Extracellular enzymes are thought to play an important role in their predation and also provide resources for discovering new antibacterial molecules. We previously isolated a myxobacterium, Corallococcus silvisoli c25j21 GDMCC 1.1387, which is predatory to plant pathogenic bacteria. In this study, we identified an endolysin-like GH19 glycoside hydrolase, C25GH19B, from the genome of c25j21. After its heterologous expression and purification from E. coli, the enzymatic properties of C25GH19B were characterized. C25GH19B showed lysozyme activity with the optimal reaction conditions at 40 °C and pH 4.5–5.0. Moreover, C25GH19B showed bacteriolytic activity against both Gram-positive and Gram-negative plant pathogenic bacteria. Our research provides not only a candidate enzyme for the development of novel biocontrol agents but also an experimental basis for further study on the function and mechanisms of extracellular enzymes in myxobacterial predation. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s13568-022-01393-y. |
format | Online Article Text |
id | pubmed-9098779 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-90987792022-05-14 A myxobacterial GH19 lysozyme with bacteriolytic activity on both Gram-positive and negative phytopathogens Li, Yueqiu Zhou, Xiaoli Zhang, Xianjiao Xu, Zhiqiang Dong, Honghong Yu, Guohui Cheng, Ping Yao, Qing Zhu, Honghui AMB Express Original Article Myxobacteria, as predatory bacteria, have good application potential in the biocontrol of pathogenic microorganisms. Extracellular enzymes are thought to play an important role in their predation and also provide resources for discovering new antibacterial molecules. We previously isolated a myxobacterium, Corallococcus silvisoli c25j21 GDMCC 1.1387, which is predatory to plant pathogenic bacteria. In this study, we identified an endolysin-like GH19 glycoside hydrolase, C25GH19B, from the genome of c25j21. After its heterologous expression and purification from E. coli, the enzymatic properties of C25GH19B were characterized. C25GH19B showed lysozyme activity with the optimal reaction conditions at 40 °C and pH 4.5–5.0. Moreover, C25GH19B showed bacteriolytic activity against both Gram-positive and Gram-negative plant pathogenic bacteria. Our research provides not only a candidate enzyme for the development of novel biocontrol agents but also an experimental basis for further study on the function and mechanisms of extracellular enzymes in myxobacterial predation. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s13568-022-01393-y. Springer Berlin Heidelberg 2022-05-12 /pmc/articles/PMC9098779/ /pubmed/35551524 http://dx.doi.org/10.1186/s13568-022-01393-y Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Original Article Li, Yueqiu Zhou, Xiaoli Zhang, Xianjiao Xu, Zhiqiang Dong, Honghong Yu, Guohui Cheng, Ping Yao, Qing Zhu, Honghui A myxobacterial GH19 lysozyme with bacteriolytic activity on both Gram-positive and negative phytopathogens |
title | A myxobacterial GH19 lysozyme with bacteriolytic activity on both Gram-positive and negative phytopathogens |
title_full | A myxobacterial GH19 lysozyme with bacteriolytic activity on both Gram-positive and negative phytopathogens |
title_fullStr | A myxobacterial GH19 lysozyme with bacteriolytic activity on both Gram-positive and negative phytopathogens |
title_full_unstemmed | A myxobacterial GH19 lysozyme with bacteriolytic activity on both Gram-positive and negative phytopathogens |
title_short | A myxobacterial GH19 lysozyme with bacteriolytic activity on both Gram-positive and negative phytopathogens |
title_sort | myxobacterial gh19 lysozyme with bacteriolytic activity on both gram-positive and negative phytopathogens |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9098779/ https://www.ncbi.nlm.nih.gov/pubmed/35551524 http://dx.doi.org/10.1186/s13568-022-01393-y |
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