Characterization of a novel N-acylhomoserine lactonase, AidP, from Antarctic Planococcus sp.
Background N-acylhomoserine lactones (AHLs) are well-studied signalling molecules produced by some Gram-negative Proteobacteria for bacterial cell-to-cell communication or quorum sensing. We have previously demonstrated the degradation of AHLs by an Antarctic bacterium, Planococcus versutus L10.15T,...
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BioMed Central
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Online Access: | https://nrl.northumbria.ac.uk/id/eprint/38094/ https://doi.org/10.1186/s12934-018-1024-6 https://nrl.northumbria.ac.uk/id/eprint/38094/1/s12934-018-1024-6.pdf |
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ftunivnorthumb:oai:nrl.northumbria.ac.uk:38094 2023-05-15T13:56:54+02:00 Characterization of a novel N-acylhomoserine lactonase, AidP, from Antarctic Planococcus sp. See-Too, Wah Seng Convey, Peter Pearce, David A. Chan, Kok-Gan 2018-11-17 text https://nrl.northumbria.ac.uk/id/eprint/38094/ https://doi.org/10.1186/s12934-018-1024-6 https://nrl.northumbria.ac.uk/id/eprint/38094/1/s12934-018-1024-6.pdf en eng BioMed Central https://nrl.northumbria.ac.uk/id/eprint/38094/1/s12934-018-1024-6.pdf See-Too, Wah Seng, Convey, Peter, Pearce, David A. and Chan, Kok-Gan (2018) Characterization of a novel N-acylhomoserine lactonase, AidP, from Antarctic Planococcus sp. Microbial Cell Factories, 17 (1). p. 179. ISSN 1475-2859 cc_by_4_0 CC-BY C700 Molecular Biology Biophysics and Biochemistry Article PeerReviewed 2018 ftunivnorthumb https://doi.org/10.1186/s12934-018-1024-6 2022-09-25T06:09:16Z Background N-acylhomoserine lactones (AHLs) are well-studied signalling molecules produced by some Gram-negative Proteobacteria for bacterial cell-to-cell communication or quorum sensing. We have previously demonstrated the degradation of AHLs by an Antarctic bacterium, Planococcus versutus L10.15T, at low temperature through the production of an AHL lactonase. In this study, we cloned the AHL lactonase gene and characterized the purified novel enzyme. Results Rapid resolution liquid chromatography analysis indicated that purified AidP possesses high AHL-degrading activity on unsubstituted, and 3-oxo substituted homoserine lactones. Liquid chromatography–mass spectrometry analysis confirmed that AidP functions as an AHL lactonase that hydrolyzes the ester bond of the homoserine lactone ring of AHLs. Multiple sequence alignment analysis and phylogenetic analysis suggested that the aidP gene encodes a novel AHL lactonase enzyme. The amino acid composition analysis of aidP and the homologous genes suggested that it might be a cold-adapted enzyme, however, the optimum temperature is 28 °C, even though the thermal stability is low (reduced drastically above 32 °C). Branch-site analysis of several aidP genes of Planococcus sp. branch on the phylogenetic trees also showed evidence of episodic positive selection of the gene in cold environments. Furthermore, we demonstrated the effects of covalent and ionic bonding, showing that Zn2+ is important for activity of AidP in vivo. The pectinolytic inhibition assay confirmed that this enzyme attenuated the pathogenicity of the plant pathogen Pectobacterium carotovorum in Chinese cabbage. Conclusion We demonstrated that AidP is effective in attenuating the pathogenicity of P. carotovorum, a plant pathogen that causes soft-rot disease. This anti-quorum sensing agent is an enzyme with low thermal stability that degrades the bacterial signalling molecules (AHLs) that are produced by many pathogens. Since the enzyme is most active below human body temperature (below 28 °C), and ... Article in Journal/Newspaper Antarc* Antarctic Northumbria University, Newcastle: Northumbria Research Link (NRL) Antarctic Microbial Cell Factories 17 1 |
institution |
Open Polar |
collection |
Northumbria University, Newcastle: Northumbria Research Link (NRL) |
op_collection_id |
ftunivnorthumb |
language |
English |
topic |
C700 Molecular Biology Biophysics and Biochemistry |
spellingShingle |
C700 Molecular Biology Biophysics and Biochemistry See-Too, Wah Seng Convey, Peter Pearce, David A. Chan, Kok-Gan Characterization of a novel N-acylhomoserine lactonase, AidP, from Antarctic Planococcus sp. |
topic_facet |
C700 Molecular Biology Biophysics and Biochemistry |
description |
Background N-acylhomoserine lactones (AHLs) are well-studied signalling molecules produced by some Gram-negative Proteobacteria for bacterial cell-to-cell communication or quorum sensing. We have previously demonstrated the degradation of AHLs by an Antarctic bacterium, Planococcus versutus L10.15T, at low temperature through the production of an AHL lactonase. In this study, we cloned the AHL lactonase gene and characterized the purified novel enzyme. Results Rapid resolution liquid chromatography analysis indicated that purified AidP possesses high AHL-degrading activity on unsubstituted, and 3-oxo substituted homoserine lactones. Liquid chromatography–mass spectrometry analysis confirmed that AidP functions as an AHL lactonase that hydrolyzes the ester bond of the homoserine lactone ring of AHLs. Multiple sequence alignment analysis and phylogenetic analysis suggested that the aidP gene encodes a novel AHL lactonase enzyme. The amino acid composition analysis of aidP and the homologous genes suggested that it might be a cold-adapted enzyme, however, the optimum temperature is 28 °C, even though the thermal stability is low (reduced drastically above 32 °C). Branch-site analysis of several aidP genes of Planococcus sp. branch on the phylogenetic trees also showed evidence of episodic positive selection of the gene in cold environments. Furthermore, we demonstrated the effects of covalent and ionic bonding, showing that Zn2+ is important for activity of AidP in vivo. The pectinolytic inhibition assay confirmed that this enzyme attenuated the pathogenicity of the plant pathogen Pectobacterium carotovorum in Chinese cabbage. Conclusion We demonstrated that AidP is effective in attenuating the pathogenicity of P. carotovorum, a plant pathogen that causes soft-rot disease. This anti-quorum sensing agent is an enzyme with low thermal stability that degrades the bacterial signalling molecules (AHLs) that are produced by many pathogens. Since the enzyme is most active below human body temperature (below 28 °C), and ... |
format |
Article in Journal/Newspaper |
author |
See-Too, Wah Seng Convey, Peter Pearce, David A. Chan, Kok-Gan |
author_facet |
See-Too, Wah Seng Convey, Peter Pearce, David A. Chan, Kok-Gan |
author_sort |
See-Too, Wah Seng |
title |
Characterization of a novel N-acylhomoserine lactonase, AidP, from Antarctic Planococcus sp. |
title_short |
Characterization of a novel N-acylhomoserine lactonase, AidP, from Antarctic Planococcus sp. |
title_full |
Characterization of a novel N-acylhomoserine lactonase, AidP, from Antarctic Planococcus sp. |
title_fullStr |
Characterization of a novel N-acylhomoserine lactonase, AidP, from Antarctic Planococcus sp. |
title_full_unstemmed |
Characterization of a novel N-acylhomoserine lactonase, AidP, from Antarctic Planococcus sp. |
title_sort |
characterization of a novel n-acylhomoserine lactonase, aidp, from antarctic planococcus sp. |
publisher |
BioMed Central |
publishDate |
2018 |
url |
https://nrl.northumbria.ac.uk/id/eprint/38094/ https://doi.org/10.1186/s12934-018-1024-6 https://nrl.northumbria.ac.uk/id/eprint/38094/1/s12934-018-1024-6.pdf |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
https://nrl.northumbria.ac.uk/id/eprint/38094/1/s12934-018-1024-6.pdf See-Too, Wah Seng, Convey, Peter, Pearce, David A. and Chan, Kok-Gan (2018) Characterization of a novel N-acylhomoserine lactonase, AidP, from Antarctic Planococcus sp. Microbial Cell Factories, 17 (1). p. 179. ISSN 1475-2859 |
op_rights |
cc_by_4_0 |
op_rightsnorm |
CC-BY |
op_doi |
https://doi.org/10.1186/s12934-018-1024-6 |
container_title |
Microbial Cell Factories |
container_volume |
17 |
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1 |
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1766264504184733696 |