Eintrag weiter verarbeiten
Heterologous Expression of the Marine-Derived Quorum Quenching Enzyme MomL Can Expand the Antibacterial Spectrum of Bacillus brevis
Gespeichert in:
Zeitschriftentitel: | Marine Drugs |
---|---|
Personen und Körperschaften: | , , , , , , |
In: | Marine Drugs, 17, 2019, 2, S. 128 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
MDPI AG
|
Schlagwörter: |
author_facet |
Zhang, Jingjing Wang, Jiayi Feng, Tao Du, Rui Tian, Xiaorong Wang, Yan Zhang, Xiao-Hua Zhang, Jingjing Wang, Jiayi Feng, Tao Du, Rui Tian, Xiaorong Wang, Yan Zhang, Xiao-Hua |
---|---|
author |
Zhang, Jingjing Wang, Jiayi Feng, Tao Du, Rui Tian, Xiaorong Wang, Yan Zhang, Xiao-Hua |
spellingShingle |
Zhang, Jingjing Wang, Jiayi Feng, Tao Du, Rui Tian, Xiaorong Wang, Yan Zhang, Xiao-Hua Marine Drugs Heterologous Expression of the Marine-Derived Quorum Quenching Enzyme MomL Can Expand the Antibacterial Spectrum of Bacillus brevis Drug Discovery Pharmacology, Toxicology and Pharmaceutics (miscellaneous) Pharmaceutical Science |
author_sort |
zhang, jingjing |
spelling |
Zhang, Jingjing Wang, Jiayi Feng, Tao Du, Rui Tian, Xiaorong Wang, Yan Zhang, Xiao-Hua 1660-3397 MDPI AG Drug Discovery Pharmacology, Toxicology and Pharmaceutics (miscellaneous) Pharmaceutical Science http://dx.doi.org/10.3390/md17020128 <jats:p>Quorum sensing (QS) is closely associated with the production of multiple virulence factors in bacterial pathogens. N-acyl homoserine lactones (AHLs) are important QS signal molecules that modulate the virulence of gram-negative pathogenic bacteria. Enzymatic degradation of AHLs to interrupt QS, termed quorum quenching (QQ), has been considered a novel strategy for reduction of pathogenicity and prevention of bacterial disease. However, the low expression levels of QQ proteins in the original host bacteria has affected the applications of these proteins. Previously, we identified a novel marine QQ enzyme, named MomL, with high activity and promising biocontrol function. In this study, we linked the target fragment momL to pNCMO2, which provided a basis for the first heterologous expression of MomL in the antifungal and anti-gram-positive-bacteria biocontrol strain Bacillus brevis, and obtaining the recombinant strain named BbMomL. The QQ activity of BbMomL was confirmed using a series of bioassays. BbMomL could not only degrade the exogenous signal molecule C6-HSL, but also the AHL signal molecules produced by the gram-negative pathogens Pectobacterium carotovorum subsp. carotovorum (Pcc) and Pseudomonas aeruginosa PAO1. In addition, BbMomL significantly reduced the secretion of pathogenic factors and the pathogenicity of Pcc and P. aeruginosa PAO1. We tested the biocontrol function of BbMomL for prevention of plant diseases in vitro. The result indicates that BbMomL has a broad antibacterial spectrum. Compared with wild-type B. brevis, BbMomL not only inhibited fungi and gram-positive bacterial pathogens but also considerably inhibited gram-negative bacterial pathogens. Moreover, the Bacillus brevis expression system has good application prospects and is an ideal host for expression and secretion of foreign proteins.</jats:p> Heterologous Expression of the Marine-Derived Quorum Quenching Enzyme MomL Can Expand the Antibacterial Spectrum of Bacillus brevis Marine Drugs |
doi_str_mv |
10.3390/md17020128 |
facet_avail |
Online Free |
finc_class_facet |
Chemie und Pharmazie |
format |
ElectronicArticle |
fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMzM5MC9tZDE3MDIwMTI4 |
id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMzM5MC9tZDE3MDIwMTI4 |
institution |
DE-Pl11 DE-Rs1 DE-14 DE-105 DE-Ch1 DE-L229 DE-D275 DE-Bn3 DE-Brt1 DE-Zwi2 DE-D161 DE-Zi4 DE-Gla1 DE-15 |
imprint |
MDPI AG, 2019 |
imprint_str_mv |
MDPI AG, 2019 |
issn |
1660-3397 |
issn_str_mv |
1660-3397 |
language |
English |
mega_collection |
MDPI AG (CrossRef) |
match_str |
zhang2019heterologousexpressionofthemarinederivedquorumquenchingenzymemomlcanexpandtheantibacterialspectrumofbacillusbrevis |
publishDateSort |
2019 |
publisher |
MDPI AG |
recordtype |
ai |
record_format |
ai |
series |
Marine Drugs |
source_id |
49 |
title |
Heterologous Expression of the Marine-Derived Quorum Quenching Enzyme MomL Can Expand the Antibacterial Spectrum of Bacillus brevis |
title_unstemmed |
Heterologous Expression of the Marine-Derived Quorum Quenching Enzyme MomL Can Expand the Antibacterial Spectrum of Bacillus brevis |
title_full |
Heterologous Expression of the Marine-Derived Quorum Quenching Enzyme MomL Can Expand the Antibacterial Spectrum of Bacillus brevis |
title_fullStr |
Heterologous Expression of the Marine-Derived Quorum Quenching Enzyme MomL Can Expand the Antibacterial Spectrum of Bacillus brevis |
title_full_unstemmed |
Heterologous Expression of the Marine-Derived Quorum Quenching Enzyme MomL Can Expand the Antibacterial Spectrum of Bacillus brevis |
title_short |
Heterologous Expression of the Marine-Derived Quorum Quenching Enzyme MomL Can Expand the Antibacterial Spectrum of Bacillus brevis |
title_sort |
heterologous expression of the marine-derived quorum quenching enzyme moml can expand the antibacterial spectrum of bacillus brevis |
topic |
Drug Discovery Pharmacology, Toxicology and Pharmaceutics (miscellaneous) Pharmaceutical Science |
url |
http://dx.doi.org/10.3390/md17020128 |
publishDate |
2019 |
physical |
128 |
description |
<jats:p>Quorum sensing (QS) is closely associated with the production of multiple virulence factors in bacterial pathogens. N-acyl homoserine lactones (AHLs) are important QS signal molecules that modulate the virulence of gram-negative pathogenic bacteria. Enzymatic degradation of AHLs to interrupt QS, termed quorum quenching (QQ), has been considered a novel strategy for reduction of pathogenicity and prevention of bacterial disease. However, the low expression levels of QQ proteins in the original host bacteria has affected the applications of these proteins. Previously, we identified a novel marine QQ enzyme, named MomL, with high activity and promising biocontrol function. In this study, we linked the target fragment momL to pNCMO2, which provided a basis for the first heterologous expression of MomL in the antifungal and anti-gram-positive-bacteria biocontrol strain Bacillus brevis, and obtaining the recombinant strain named BbMomL. The QQ activity of BbMomL was confirmed using a series of bioassays. BbMomL could not only degrade the exogenous signal molecule C6-HSL, but also the AHL signal molecules produced by the gram-negative pathogens Pectobacterium carotovorum subsp. carotovorum (Pcc) and Pseudomonas aeruginosa PAO1. In addition, BbMomL significantly reduced the secretion of pathogenic factors and the pathogenicity of Pcc and P. aeruginosa PAO1. We tested the biocontrol function of BbMomL for prevention of plant diseases in vitro. The result indicates that BbMomL has a broad antibacterial spectrum. Compared with wild-type B. brevis, BbMomL not only inhibited fungi and gram-positive bacterial pathogens but also considerably inhibited gram-negative bacterial pathogens. Moreover, the Bacillus brevis expression system has good application prospects and is an ideal host for expression and secretion of foreign proteins.</jats:p> |
container_issue |
2 |
container_start_page |
0 |
container_title |
Marine Drugs |
container_volume |
17 |
format_de105 |
Article, E-Article |
format_de14 |
Article, E-Article |
format_de15 |
Article, E-Article |
format_de520 |
Article, E-Article |
format_de540 |
Article, E-Article |
format_dech1 |
Article, E-Article |
format_ded117 |
Article, E-Article |
format_degla1 |
E-Article |
format_del152 |
Buch |
format_del189 |
Article, E-Article |
format_dezi4 |
Article |
format_dezwi2 |
Article, E-Article |
format_finc |
Article, E-Article |
format_nrw |
Article, E-Article |
_version_ |
1792338849347665922 |
geogr_code |
not assigned |
last_indexed |
2024-03-01T15:38:45.479Z |
geogr_code_person |
not assigned |
openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=Heterologous+Expression+of+the+Marine-Derived+Quorum+Quenching+Enzyme+MomL+Can+Expand+the+Antibacterial+Spectrum+of+Bacillus+brevis&rft.date=2019-02-21&genre=article&issn=1660-3397&volume=17&issue=2&pages=128&jtitle=Marine+Drugs&atitle=Heterologous+Expression+of+the+Marine-Derived+Quorum+Quenching+Enzyme+MomL+Can+Expand+the+Antibacterial+Spectrum+of+Bacillus+brevis&aulast=Zhang&aufirst=Xiao-Hua&rft_id=info%3Adoi%2F10.3390%2Fmd17020128&rft.language%5B0%5D=eng |
SOLR | |
_version_ | 1792338849347665922 |
author | Zhang, Jingjing, Wang, Jiayi, Feng, Tao, Du, Rui, Tian, Xiaorong, Wang, Yan, Zhang, Xiao-Hua |
author_facet | Zhang, Jingjing, Wang, Jiayi, Feng, Tao, Du, Rui, Tian, Xiaorong, Wang, Yan, Zhang, Xiao-Hua, Zhang, Jingjing, Wang, Jiayi, Feng, Tao, Du, Rui, Tian, Xiaorong, Wang, Yan, Zhang, Xiao-Hua |
author_sort | zhang, jingjing |
container_issue | 2 |
container_start_page | 0 |
container_title | Marine Drugs |
container_volume | 17 |
description | <jats:p>Quorum sensing (QS) is closely associated with the production of multiple virulence factors in bacterial pathogens. N-acyl homoserine lactones (AHLs) are important QS signal molecules that modulate the virulence of gram-negative pathogenic bacteria. Enzymatic degradation of AHLs to interrupt QS, termed quorum quenching (QQ), has been considered a novel strategy for reduction of pathogenicity and prevention of bacterial disease. However, the low expression levels of QQ proteins in the original host bacteria has affected the applications of these proteins. Previously, we identified a novel marine QQ enzyme, named MomL, with high activity and promising biocontrol function. In this study, we linked the target fragment momL to pNCMO2, which provided a basis for the first heterologous expression of MomL in the antifungal and anti-gram-positive-bacteria biocontrol strain Bacillus brevis, and obtaining the recombinant strain named BbMomL. The QQ activity of BbMomL was confirmed using a series of bioassays. BbMomL could not only degrade the exogenous signal molecule C6-HSL, but also the AHL signal molecules produced by the gram-negative pathogens Pectobacterium carotovorum subsp. carotovorum (Pcc) and Pseudomonas aeruginosa PAO1. In addition, BbMomL significantly reduced the secretion of pathogenic factors and the pathogenicity of Pcc and P. aeruginosa PAO1. We tested the biocontrol function of BbMomL for prevention of plant diseases in vitro. The result indicates that BbMomL has a broad antibacterial spectrum. Compared with wild-type B. brevis, BbMomL not only inhibited fungi and gram-positive bacterial pathogens but also considerably inhibited gram-negative bacterial pathogens. Moreover, the Bacillus brevis expression system has good application prospects and is an ideal host for expression and secretion of foreign proteins.</jats:p> |
doi_str_mv | 10.3390/md17020128 |
facet_avail | Online, Free |
finc_class_facet | Chemie und Pharmazie |
format | ElectronicArticle |
format_de105 | Article, E-Article |
format_de14 | Article, E-Article |
format_de15 | Article, E-Article |
format_de520 | Article, E-Article |
format_de540 | Article, E-Article |
format_dech1 | Article, E-Article |
format_ded117 | Article, E-Article |
format_degla1 | E-Article |
format_del152 | Buch |
format_del189 | Article, E-Article |
format_dezi4 | Article |
format_dezwi2 | Article, E-Article |
format_finc | Article, E-Article |
format_nrw | Article, E-Article |
geogr_code | not assigned |
geogr_code_person | not assigned |
id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMzM5MC9tZDE3MDIwMTI4 |
imprint | MDPI AG, 2019 |
imprint_str_mv | MDPI AG, 2019 |
institution | DE-Pl11, DE-Rs1, DE-14, DE-105, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Zi4, DE-Gla1, DE-15 |
issn | 1660-3397 |
issn_str_mv | 1660-3397 |
language | English |
last_indexed | 2024-03-01T15:38:45.479Z |
match_str | zhang2019heterologousexpressionofthemarinederivedquorumquenchingenzymemomlcanexpandtheantibacterialspectrumofbacillusbrevis |
mega_collection | MDPI AG (CrossRef) |
physical | 128 |
publishDate | 2019 |
publishDateSort | 2019 |
publisher | MDPI AG |
record_format | ai |
recordtype | ai |
series | Marine Drugs |
source_id | 49 |
spelling | Zhang, Jingjing Wang, Jiayi Feng, Tao Du, Rui Tian, Xiaorong Wang, Yan Zhang, Xiao-Hua 1660-3397 MDPI AG Drug Discovery Pharmacology, Toxicology and Pharmaceutics (miscellaneous) Pharmaceutical Science http://dx.doi.org/10.3390/md17020128 <jats:p>Quorum sensing (QS) is closely associated with the production of multiple virulence factors in bacterial pathogens. N-acyl homoserine lactones (AHLs) are important QS signal molecules that modulate the virulence of gram-negative pathogenic bacteria. Enzymatic degradation of AHLs to interrupt QS, termed quorum quenching (QQ), has been considered a novel strategy for reduction of pathogenicity and prevention of bacterial disease. However, the low expression levels of QQ proteins in the original host bacteria has affected the applications of these proteins. Previously, we identified a novel marine QQ enzyme, named MomL, with high activity and promising biocontrol function. In this study, we linked the target fragment momL to pNCMO2, which provided a basis for the first heterologous expression of MomL in the antifungal and anti-gram-positive-bacteria biocontrol strain Bacillus brevis, and obtaining the recombinant strain named BbMomL. The QQ activity of BbMomL was confirmed using a series of bioassays. BbMomL could not only degrade the exogenous signal molecule C6-HSL, but also the AHL signal molecules produced by the gram-negative pathogens Pectobacterium carotovorum subsp. carotovorum (Pcc) and Pseudomonas aeruginosa PAO1. In addition, BbMomL significantly reduced the secretion of pathogenic factors and the pathogenicity of Pcc and P. aeruginosa PAO1. We tested the biocontrol function of BbMomL for prevention of plant diseases in vitro. The result indicates that BbMomL has a broad antibacterial spectrum. Compared with wild-type B. brevis, BbMomL not only inhibited fungi and gram-positive bacterial pathogens but also considerably inhibited gram-negative bacterial pathogens. Moreover, the Bacillus brevis expression system has good application prospects and is an ideal host for expression and secretion of foreign proteins.</jats:p> Heterologous Expression of the Marine-Derived Quorum Quenching Enzyme MomL Can Expand the Antibacterial Spectrum of Bacillus brevis Marine Drugs |
spellingShingle | Zhang, Jingjing, Wang, Jiayi, Feng, Tao, Du, Rui, Tian, Xiaorong, Wang, Yan, Zhang, Xiao-Hua, Marine Drugs, Heterologous Expression of the Marine-Derived Quorum Quenching Enzyme MomL Can Expand the Antibacterial Spectrum of Bacillus brevis, Drug Discovery, Pharmacology, Toxicology and Pharmaceutics (miscellaneous), Pharmaceutical Science |
title | Heterologous Expression of the Marine-Derived Quorum Quenching Enzyme MomL Can Expand the Antibacterial Spectrum of Bacillus brevis |
title_full | Heterologous Expression of the Marine-Derived Quorum Quenching Enzyme MomL Can Expand the Antibacterial Spectrum of Bacillus brevis |
title_fullStr | Heterologous Expression of the Marine-Derived Quorum Quenching Enzyme MomL Can Expand the Antibacterial Spectrum of Bacillus brevis |
title_full_unstemmed | Heterologous Expression of the Marine-Derived Quorum Quenching Enzyme MomL Can Expand the Antibacterial Spectrum of Bacillus brevis |
title_short | Heterologous Expression of the Marine-Derived Quorum Quenching Enzyme MomL Can Expand the Antibacterial Spectrum of Bacillus brevis |
title_sort | heterologous expression of the marine-derived quorum quenching enzyme moml can expand the antibacterial spectrum of bacillus brevis |
title_unstemmed | Heterologous Expression of the Marine-Derived Quorum Quenching Enzyme MomL Can Expand the Antibacterial Spectrum of Bacillus brevis |
topic | Drug Discovery, Pharmacology, Toxicology and Pharmaceutics (miscellaneous), Pharmaceutical Science |
url | http://dx.doi.org/10.3390/md17020128 |