A systematic analysis of the role of GGDEF-EAL domain proteins in virulence and motility in Xanthomonas oryzae pv. oryzicola

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dc.contributor.author Wei, Chao
dc.contributor.author Jiang, Wendi
dc.contributor.author Zhao, Mengran
dc.contributor.author Ling, Junjie
dc.contributor.author Zeng, Xin
dc.contributor.author Deng, Jun
dc.contributor.author Jin, Dongli
dc.contributor.author Dow, J. Maxwell
dc.contributor.author Sun, Wenxian
dc.date.accessioned 2016-10-11T08:47:08Z
dc.date.available 2016-10-11T08:47:08Z
dc.date.issued 2016-04-07
dc.identifier.citation WEI, C., JIANG, W., ZHAO, M., LING, J., ZENG, X., DENG, J., JIN, D., DOW, J. M. & SUN, W. (2016) 'A systematic analysis of the role of GGDEF-EAL domain proteins in virulence and motility in Xanthomonas oryzae pv. oryzicola', Scientific Reports, 6, 23769 (14 pp). doi:10.1038/srep23769 en
dc.identifier.issued 6 en
dc.identifier.startpage 1 en
dc.identifier.endpage 14 en
dc.identifier.issn 2045-2322
dc.identifier.uri http://hdl.handle.net/10468/3173
dc.identifier.doi 10.1038/srep23769
dc.description.abstract The second messenger c-di-GMP is implicated in regulation of various aspects of the lifestyles and virulence of Gram-negative bacteria. Cyclic di-GMP is formed by diguanylate cyclases with a GGDEF domain and degraded by phosphodiesterases with either an EAL or HD-GYP domain. Proteins with tandem GGDEF-EAL domains occur in many bacteria, where they may be involved in c-di-GMP turnover or act as enzymatically-inactive c-di-GMP effectors. Here, we report a systematic study of the regulatory action of the eleven GGDEF-EAL proteins in Xanthomonas oryzae pv. oryzicola, an important rice pathogen causing bacterial leaf streak. Mutational analysis revealed that XOC_2335 and XOC_2393 positively regulate bacterial swimming motility, while XOC_2102, XOC_2393 and XOC_4190 negatively control sliding motility. The ΔXOC_2335/XOC_2393 mutant that had a higher intracellular c-di-GMP level than the wild type and the ΔXOC_4190 mutant exhibited reduced virulence to rice after pressure inoculation. In vitro purified XOC_4190 and XOC_2102 have little or no diguanylate cyclase or phosphodiesterase activity, which is consistent with unaltered c-di-GMP concentration in ΔXOC_4190. Nevertheless, both proteins can bind to c-di-GMP with high affinity, indicating a potential role as c-di-GMP effectors. Overall our findings advance understanding of c-di-GMP signaling and its links to virulence in an important rice pathogen. en
dc.description.sponsorship Special Fund for Agro-Scientific Research in the Public Interest of China (Grant 201303015); National Natural Science Foundation of China (Grant 31272007); National High Technology Research and Development Program of China (Grant 2012AA100703); 111 project (Grant B13006) en
dc.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher Nature Publishing Group en
dc.rights © 2016, the Authors. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ en
dc.rights.uri http://creativecommons.org/licenses/by/4.0/ en
dc.subject Virulence en
dc.subject Proteins en
dc.subject Motility en
dc.subject Bacteria en
dc.subject Pathogen en
dc.title A systematic analysis of the role of GGDEF-EAL domain proteins in virulence and motility in Xanthomonas oryzae pv. oryzicola en
dc.type Article (peer-reviewed) en
dc.internal.authorcontactother Max Dow, Microbiology, University College Cork, Cork, Ireland. +353-21-490-3000 Email: M.Dow@ucc.ie en
dc.internal.availability Full text available en
dc.description.version Published Version en
dc.contributor.funder Special Fund for Agro-Scientific Research in the Public Interest of China
dc.contributor.funder National Natural Science Foundation of China
dc.contributor.funder National High Technology Research and Development Program of China
dc.contributor.funder 111 project
dc.description.status Peer reviewed en
dc.identifier.journaltitle Scientific Reports en
dc.internal.IRISemailaddress M.Dow@ucc.ie
dc.internal.IRISemailaddress m.dow@ucc.ie en
dc.identifier.articleid 23769


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© 2016, the Authors. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ Except where otherwise noted, this item's license is described as © 2016, the Authors. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
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