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Identification of a Key Amino Acid of LuxS Involved in AI-2 Production in Campylobacter jejuni
Autoinducer-2 (AI-2) mediated quorum sensing has been associated with the expression of virulence factors in a number of pathogenic organisms and has been demonstrated to play a role in motility and cytolethal distending toxin (cdt) production in Campylobacter jejuni. We have initiated the work to d...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Public Library of Science
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3019222/ https://www.ncbi.nlm.nih.gov/pubmed/21264316 http://dx.doi.org/10.1371/journal.pone.0015876 |
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author | Plummer, Paul Zhu, Jinge Akiba, Masato Pei, Dehua Zhang, Qijing |
author_facet | Plummer, Paul Zhu, Jinge Akiba, Masato Pei, Dehua Zhang, Qijing |
author_sort | Plummer, Paul |
collection | PubMed |
description | Autoinducer-2 (AI-2) mediated quorum sensing has been associated with the expression of virulence factors in a number of pathogenic organisms and has been demonstrated to play a role in motility and cytolethal distending toxin (cdt) production in Campylobacter jejuni. We have initiated the work to determine the molecular basis of AI-2 synthesis and the biological functions of quorum sensing in C. jejuni. In this work, two naturally occurring variants of C. jejuni 81116 were identified, one producing high-levels of AI-2 while the other is defective in AI-2 synthesis. Sequence analysis revealed a G92D mutation in the luxS gene of the defective variant. Complementation of the AI-2(−) variant with a plasmid encoded copy of the wild-type luxS gene or reversion of the G92D mutation by site-directed mutagenesis fully restored AI-2 production by the variant. These results indicate that the G92D mutation alone is responsible for the loss of AI-2 activity in C. jejuni. Kinetic analyses showed that the G92D LuxS has a ∼100-fold reduced catalytic activity relative to the wild-type enzyme. Findings from this study identify a previously undescribed amino acid that is essential for AI-2 production by LuxS and provide a unique isogenic pair of naturally occurring variants for us to dissect the functions of AI-2 mediated quorum sensing in Campylobacter. |
format | Text |
id | pubmed-3019222 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-30192222011-01-24 Identification of a Key Amino Acid of LuxS Involved in AI-2 Production in Campylobacter jejuni Plummer, Paul Zhu, Jinge Akiba, Masato Pei, Dehua Zhang, Qijing PLoS One Research Article Autoinducer-2 (AI-2) mediated quorum sensing has been associated with the expression of virulence factors in a number of pathogenic organisms and has been demonstrated to play a role in motility and cytolethal distending toxin (cdt) production in Campylobacter jejuni. We have initiated the work to determine the molecular basis of AI-2 synthesis and the biological functions of quorum sensing in C. jejuni. In this work, two naturally occurring variants of C. jejuni 81116 were identified, one producing high-levels of AI-2 while the other is defective in AI-2 synthesis. Sequence analysis revealed a G92D mutation in the luxS gene of the defective variant. Complementation of the AI-2(−) variant with a plasmid encoded copy of the wild-type luxS gene or reversion of the G92D mutation by site-directed mutagenesis fully restored AI-2 production by the variant. These results indicate that the G92D mutation alone is responsible for the loss of AI-2 activity in C. jejuni. Kinetic analyses showed that the G92D LuxS has a ∼100-fold reduced catalytic activity relative to the wild-type enzyme. Findings from this study identify a previously undescribed amino acid that is essential for AI-2 production by LuxS and provide a unique isogenic pair of naturally occurring variants for us to dissect the functions of AI-2 mediated quorum sensing in Campylobacter. Public Library of Science 2011-01-11 /pmc/articles/PMC3019222/ /pubmed/21264316 http://dx.doi.org/10.1371/journal.pone.0015876 Text en Plummer et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Plummer, Paul Zhu, Jinge Akiba, Masato Pei, Dehua Zhang, Qijing Identification of a Key Amino Acid of LuxS Involved in AI-2 Production in Campylobacter jejuni |
title | Identification of a Key Amino Acid of LuxS Involved in AI-2 Production in Campylobacter jejuni
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title_full | Identification of a Key Amino Acid of LuxS Involved in AI-2 Production in Campylobacter jejuni
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title_fullStr | Identification of a Key Amino Acid of LuxS Involved in AI-2 Production in Campylobacter jejuni
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title_full_unstemmed | Identification of a Key Amino Acid of LuxS Involved in AI-2 Production in Campylobacter jejuni
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title_short | Identification of a Key Amino Acid of LuxS Involved in AI-2 Production in Campylobacter jejuni
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title_sort | identification of a key amino acid of luxs involved in ai-2 production in campylobacter jejuni |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3019222/ https://www.ncbi.nlm.nih.gov/pubmed/21264316 http://dx.doi.org/10.1371/journal.pone.0015876 |
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