HqiA, a novel quorum-quenching enzyme which expands the AHL lactonase family

Abstract The screening of a metagenomic library of 250,000 clones generated from a hypersaline soil (Spain) allowed us to identify a single positive clone which confers the ability to degrade N-acyl homoserine lactones (AHLs). The sequencing of the fosmid revealed a 42,318 bp environmental insert ch...

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Autores principales: Marta Torres, Stéphane Uroz, Rafael Salto, Laure Fauchery, Emilia Quesada, Inmaculada Llamas
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Lenguaje:EN
Publicado: Nature Portfolio 2017
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Acceso en línea:https://doaj.org/article/84520fc4c60c436d88e1415a18022cf4
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spelling oai:doaj.org-article:84520fc4c60c436d88e1415a18022cf42021-12-02T12:32:32ZHqiA, a novel quorum-quenching enzyme which expands the AHL lactonase family10.1038/s41598-017-01176-72045-2322https://doaj.org/article/84520fc4c60c436d88e1415a18022cf42017-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-01176-7https://doaj.org/toc/2045-2322Abstract The screening of a metagenomic library of 250,000 clones generated from a hypersaline soil (Spain) allowed us to identify a single positive clone which confers the ability to degrade N-acyl homoserine lactones (AHLs). The sequencing of the fosmid revealed a 42,318 bp environmental insert characterized by 46 ORFs. The subcloning of these ORFs demonstrated that a single gene (hqiA) allowed AHL degradation. Enzymatic analysis using purified HqiA and HPLC/MS revealed that this protein has lactonase activity on a broad range of AHLs. The introduction of hqiA in the plant pathogen Pectobacterium carotovorum efficiently interfered with both the synthesis of AHLs and quorum-sensing regulated functions, such as swarming motility and the production of maceration enzymes. Bioinformatic analyses highlighted that HqiA showed no sequence homology with the known prototypic AHL lactonases or acylases, thus expanding the AHL-degrading enzymes with a new family related to the cysteine hydrolase (CHase) group. The complete sequence analysis of the fosmid showed that 31 ORFs out of the 46 identified were related to Deltaproteobacteria, whilst many intercalated ORFs presented high homology with other taxa. In this sense, hqiA appeared to be assigned to the Hyphomonas genus (Alphaproteobacteria), suggesting that horizontal gene transfer had occurred.Marta TorresStéphane UrozRafael SaltoLaure FaucheryEmilia QuesadaInmaculada LlamasNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-15 (2017)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Marta Torres
Stéphane Uroz
Rafael Salto
Laure Fauchery
Emilia Quesada
Inmaculada Llamas
HqiA, a novel quorum-quenching enzyme which expands the AHL lactonase family
description Abstract The screening of a metagenomic library of 250,000 clones generated from a hypersaline soil (Spain) allowed us to identify a single positive clone which confers the ability to degrade N-acyl homoserine lactones (AHLs). The sequencing of the fosmid revealed a 42,318 bp environmental insert characterized by 46 ORFs. The subcloning of these ORFs demonstrated that a single gene (hqiA) allowed AHL degradation. Enzymatic analysis using purified HqiA and HPLC/MS revealed that this protein has lactonase activity on a broad range of AHLs. The introduction of hqiA in the plant pathogen Pectobacterium carotovorum efficiently interfered with both the synthesis of AHLs and quorum-sensing regulated functions, such as swarming motility and the production of maceration enzymes. Bioinformatic analyses highlighted that HqiA showed no sequence homology with the known prototypic AHL lactonases or acylases, thus expanding the AHL-degrading enzymes with a new family related to the cysteine hydrolase (CHase) group. The complete sequence analysis of the fosmid showed that 31 ORFs out of the 46 identified were related to Deltaproteobacteria, whilst many intercalated ORFs presented high homology with other taxa. In this sense, hqiA appeared to be assigned to the Hyphomonas genus (Alphaproteobacteria), suggesting that horizontal gene transfer had occurred.
format article
author Marta Torres
Stéphane Uroz
Rafael Salto
Laure Fauchery
Emilia Quesada
Inmaculada Llamas
author_facet Marta Torres
Stéphane Uroz
Rafael Salto
Laure Fauchery
Emilia Quesada
Inmaculada Llamas
author_sort Marta Torres
title HqiA, a novel quorum-quenching enzyme which expands the AHL lactonase family
title_short HqiA, a novel quorum-quenching enzyme which expands the AHL lactonase family
title_full HqiA, a novel quorum-quenching enzyme which expands the AHL lactonase family
title_fullStr HqiA, a novel quorum-quenching enzyme which expands the AHL lactonase family
title_full_unstemmed HqiA, a novel quorum-quenching enzyme which expands the AHL lactonase family
title_sort hqia, a novel quorum-quenching enzyme which expands the ahl lactonase family
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/84520fc4c60c436d88e1415a18022cf4
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