LuxS and quorum-sensing in Campylobacter

Several intercellular bacterial communication mechanisms have been identified in a broad range of bacterial species. These systems, collectively termed quorum-sensing systems, have been demonstrated to play significant roles in a variety of bacterial processes including motility, biofilm formation,...

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Main Author: Paul ePlummer
Format: Article
Language:English
Published: Frontiers Media S.A. 2012-03-01
Series:Frontiers in Cellular and Infection Microbiology
Subjects:
Online Access:http://journal.frontiersin.org/Journal/10.3389/fcimb.2012.00022/full
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author Paul ePlummer
Paul ePlummer
author_facet Paul ePlummer
Paul ePlummer
author_sort Paul ePlummer
collection DOAJ
description Several intercellular bacterial communication mechanisms have been identified in a broad range of bacterial species. These systems, collectively termed quorum-sensing systems, have been demonstrated to play significant roles in a variety of bacterial processes including motility, biofilm formation, expression of virulence genes and animal colonization. Campylobacter jejuni is known to poses a LuxS/ autoinducer-2 mediated system that has been partially characterized over the last decade. AI-2 is formed as a byproduct of the activated methyl recycling pathway, specifically by the LuxS enzyme. Previous work in our laboratory and that of others has demonstrated that this gene is involved in a variety of physiologic pathways of C. jejuni including motility, autoagglutination, CDT expression, flagellar expression, oxidative stress and animal colonization. This review article will summarize the current research associated with LuxS in C. jejuni and will provide insights into the role of this system in the metabolism and intercellular communication of this organism. Additionally, the evidence for other quorum sensing pathways in Campylobacter will be discussed.
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spelling doaj.art-4b53f85c0d1c45d0973692b6d6486a792022-12-22T00:01:40ZengFrontiers Media S.A.Frontiers in Cellular and Infection Microbiology2235-29882012-03-01210.3389/fcimb.2012.0002218106LuxS and quorum-sensing in CampylobacterPaul ePlummer0Paul ePlummer1Iowa State UniversityIowa State UniversitySeveral intercellular bacterial communication mechanisms have been identified in a broad range of bacterial species. These systems, collectively termed quorum-sensing systems, have been demonstrated to play significant roles in a variety of bacterial processes including motility, biofilm formation, expression of virulence genes and animal colonization. Campylobacter jejuni is known to poses a LuxS/ autoinducer-2 mediated system that has been partially characterized over the last decade. AI-2 is formed as a byproduct of the activated methyl recycling pathway, specifically by the LuxS enzyme. Previous work in our laboratory and that of others has demonstrated that this gene is involved in a variety of physiologic pathways of C. jejuni including motility, autoagglutination, CDT expression, flagellar expression, oxidative stress and animal colonization. This review article will summarize the current research associated with LuxS in C. jejuni and will provide insights into the role of this system in the metabolism and intercellular communication of this organism. Additionally, the evidence for other quorum sensing pathways in Campylobacter will be discussed.http://journal.frontiersin.org/Journal/10.3389/fcimb.2012.00022/fullCampylobacterVirulenceLuxSHSLquorum-sensingAI-2
spellingShingle Paul ePlummer
Paul ePlummer
LuxS and quorum-sensing in Campylobacter
Frontiers in Cellular and Infection Microbiology
Campylobacter
Virulence
LuxS
HSL
quorum-sensing
AI-2
title LuxS and quorum-sensing in Campylobacter
title_full LuxS and quorum-sensing in Campylobacter
title_fullStr LuxS and quorum-sensing in Campylobacter
title_full_unstemmed LuxS and quorum-sensing in Campylobacter
title_short LuxS and quorum-sensing in Campylobacter
title_sort luxs and quorum sensing in campylobacter
topic Campylobacter
Virulence
LuxS
HSL
quorum-sensing
AI-2
url http://journal.frontiersin.org/Journal/10.3389/fcimb.2012.00022/full
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