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The type III protein secretion system contributes to Xanthomonas citri subsp. citri biofilm formation
BACKGROUND: Several bacterial plant pathogens colonize their hosts through the secretion of effector proteins by a Type III protein secretion system (T3SS). The role of T3SS in bacterial pathogenesis is well established but whether this system is involved in multicellular processes, such as bacteria...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4021560/ https://www.ncbi.nlm.nih.gov/pubmed/24742141 http://dx.doi.org/10.1186/1471-2180-14-96 |
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author | Zimaro, Tamara Thomas, Ludivine Marondedze, Claudius Sgro, Germán G Garofalo, Cecilia G Ficarra, Florencia A Gehring, Chris Ottado, Jorgelina Gottig, Natalia |
author_facet | Zimaro, Tamara Thomas, Ludivine Marondedze, Claudius Sgro, Germán G Garofalo, Cecilia G Ficarra, Florencia A Gehring, Chris Ottado, Jorgelina Gottig, Natalia |
author_sort | Zimaro, Tamara |
collection | PubMed |
description | BACKGROUND: Several bacterial plant pathogens colonize their hosts through the secretion of effector proteins by a Type III protein secretion system (T3SS). The role of T3SS in bacterial pathogenesis is well established but whether this system is involved in multicellular processes, such as bacterial biofilm formation has not been elucidated. Here, the phytopathogen Xanthomonas citri subsp. citri (X. citri) was used as a model to gain further insights about the role of the T3SS in biofilm formation. RESULTS: The capacity of biofilm formation of different X. citri T3SS mutants was compared to the wild type strain and it was observed that this secretion system was necessary for this process. Moreover, the T3SS mutants adhered proficiently to leaf surfaces but were impaired in leaf-associated growth. A proteomic study of biofilm cells showed that the lack of the T3SS causes changes in the expression of proteins involved in metabolic processes, energy generation, exopolysaccharide (EPS) production and bacterial motility as well as outer membrane proteins. Furthermore, EPS production and bacterial motility were also altered in the T3SS mutants. CONCLUSIONS: Our results indicate a novel role for T3SS in X. citri in the modulation of biofilm formation. Since this process increases X. citri virulence, this study reveals new functions of T3SS in pathogenesis. |
format | Online Article Text |
id | pubmed-4021560 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-40215602014-05-16 The type III protein secretion system contributes to Xanthomonas citri subsp. citri biofilm formation Zimaro, Tamara Thomas, Ludivine Marondedze, Claudius Sgro, Germán G Garofalo, Cecilia G Ficarra, Florencia A Gehring, Chris Ottado, Jorgelina Gottig, Natalia BMC Microbiol Research Article BACKGROUND: Several bacterial plant pathogens colonize their hosts through the secretion of effector proteins by a Type III protein secretion system (T3SS). The role of T3SS in bacterial pathogenesis is well established but whether this system is involved in multicellular processes, such as bacterial biofilm formation has not been elucidated. Here, the phytopathogen Xanthomonas citri subsp. citri (X. citri) was used as a model to gain further insights about the role of the T3SS in biofilm formation. RESULTS: The capacity of biofilm formation of different X. citri T3SS mutants was compared to the wild type strain and it was observed that this secretion system was necessary for this process. Moreover, the T3SS mutants adhered proficiently to leaf surfaces but were impaired in leaf-associated growth. A proteomic study of biofilm cells showed that the lack of the T3SS causes changes in the expression of proteins involved in metabolic processes, energy generation, exopolysaccharide (EPS) production and bacterial motility as well as outer membrane proteins. Furthermore, EPS production and bacterial motility were also altered in the T3SS mutants. CONCLUSIONS: Our results indicate a novel role for T3SS in X. citri in the modulation of biofilm formation. Since this process increases X. citri virulence, this study reveals new functions of T3SS in pathogenesis. BioMed Central 2014-04-18 /pmc/articles/PMC4021560/ /pubmed/24742141 http://dx.doi.org/10.1186/1471-2180-14-96 Text en Copyright © 2014 Zimaro et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Zimaro, Tamara Thomas, Ludivine Marondedze, Claudius Sgro, Germán G Garofalo, Cecilia G Ficarra, Florencia A Gehring, Chris Ottado, Jorgelina Gottig, Natalia The type III protein secretion system contributes to Xanthomonas citri subsp. citri biofilm formation |
title | The type III protein secretion system contributes to Xanthomonas citri subsp. citri biofilm formation |
title_full | The type III protein secretion system contributes to Xanthomonas citri subsp. citri biofilm formation |
title_fullStr | The type III protein secretion system contributes to Xanthomonas citri subsp. citri biofilm formation |
title_full_unstemmed | The type III protein secretion system contributes to Xanthomonas citri subsp. citri biofilm formation |
title_short | The type III protein secretion system contributes to Xanthomonas citri subsp. citri biofilm formation |
title_sort | type iii protein secretion system contributes to xanthomonas citri subsp. citri biofilm formation |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4021560/ https://www.ncbi.nlm.nih.gov/pubmed/24742141 http://dx.doi.org/10.1186/1471-2180-14-96 |
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