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VapD in Xylella fastidiosa Is a Thermostable Protein with Ribonuclease Activity
Xylella fastidiosa strain 9a5c is a gram-negative phytopathogen that is the causal agent of citrus variegated chlorosis (CVC), a disease that is responsible for economic losses in Brazilian agriculture. The most well-known mechanism of pathogenicity for this bacterial pathogen is xylem vessel occlus...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4687846/ https://www.ncbi.nlm.nih.gov/pubmed/26694028 http://dx.doi.org/10.1371/journal.pone.0145765 |
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author | Mendes, Juliano S. Santiago, André da S. Toledo, Marcelo A. S. Rosselli-Murai, Luciana K. Favaro, Marianna T. P. Santos, Clelton A. Horta, Maria Augusta C. Crucello, Aline Beloti, Lilian L. Romero, Fabian Tasic, Ljubica de Souza, Alessandra A. de Souza, Anete P. |
author_facet | Mendes, Juliano S. Santiago, André da S. Toledo, Marcelo A. S. Rosselli-Murai, Luciana K. Favaro, Marianna T. P. Santos, Clelton A. Horta, Maria Augusta C. Crucello, Aline Beloti, Lilian L. Romero, Fabian Tasic, Ljubica de Souza, Alessandra A. de Souza, Anete P. |
author_sort | Mendes, Juliano S. |
collection | PubMed |
description | Xylella fastidiosa strain 9a5c is a gram-negative phytopathogen that is the causal agent of citrus variegated chlorosis (CVC), a disease that is responsible for economic losses in Brazilian agriculture. The most well-known mechanism of pathogenicity for this bacterial pathogen is xylem vessel occlusion, which results from bacterial movement and the formation of biofilms. The molecular mechanisms underlying the virulence caused by biofilm formation are unknown. Here, we provide evidence showing that virulence-associated protein D in X. fastidiosa (Xf-VapD) is a thermostable protein with ribonuclease activity. Moreover, protein expression analyses in two X. fastidiosa strains, including virulent (Xf9a5c) and nonpathogenic (XfJ1a12) strains, showed that Xf-VapD was expressed during all phases of development in both strains and that increased expression was observed in Xf9a5c during biofilm growth. This study is an important step toward characterizing and improving our understanding of the biological significance of Xf-VapD and its potential functions in the CVC pathosystem. |
format | Online Article Text |
id | pubmed-4687846 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-46878462015-12-31 VapD in Xylella fastidiosa Is a Thermostable Protein with Ribonuclease Activity Mendes, Juliano S. Santiago, André da S. Toledo, Marcelo A. S. Rosselli-Murai, Luciana K. Favaro, Marianna T. P. Santos, Clelton A. Horta, Maria Augusta C. Crucello, Aline Beloti, Lilian L. Romero, Fabian Tasic, Ljubica de Souza, Alessandra A. de Souza, Anete P. PLoS One Research Article Xylella fastidiosa strain 9a5c is a gram-negative phytopathogen that is the causal agent of citrus variegated chlorosis (CVC), a disease that is responsible for economic losses in Brazilian agriculture. The most well-known mechanism of pathogenicity for this bacterial pathogen is xylem vessel occlusion, which results from bacterial movement and the formation of biofilms. The molecular mechanisms underlying the virulence caused by biofilm formation are unknown. Here, we provide evidence showing that virulence-associated protein D in X. fastidiosa (Xf-VapD) is a thermostable protein with ribonuclease activity. Moreover, protein expression analyses in two X. fastidiosa strains, including virulent (Xf9a5c) and nonpathogenic (XfJ1a12) strains, showed that Xf-VapD was expressed during all phases of development in both strains and that increased expression was observed in Xf9a5c during biofilm growth. This study is an important step toward characterizing and improving our understanding of the biological significance of Xf-VapD and its potential functions in the CVC pathosystem. Public Library of Science 2015-12-22 /pmc/articles/PMC4687846/ /pubmed/26694028 http://dx.doi.org/10.1371/journal.pone.0145765 Text en © 2015 Mendes 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 Mendes, Juliano S. Santiago, André da S. Toledo, Marcelo A. S. Rosselli-Murai, Luciana K. Favaro, Marianna T. P. Santos, Clelton A. Horta, Maria Augusta C. Crucello, Aline Beloti, Lilian L. Romero, Fabian Tasic, Ljubica de Souza, Alessandra A. de Souza, Anete P. VapD in Xylella fastidiosa Is a Thermostable Protein with Ribonuclease Activity |
title | VapD in Xylella fastidiosa Is a Thermostable Protein with Ribonuclease Activity |
title_full | VapD in Xylella fastidiosa Is a Thermostable Protein with Ribonuclease Activity |
title_fullStr | VapD in Xylella fastidiosa Is a Thermostable Protein with Ribonuclease Activity |
title_full_unstemmed | VapD in Xylella fastidiosa Is a Thermostable Protein with Ribonuclease Activity |
title_short | VapD in Xylella fastidiosa Is a Thermostable Protein with Ribonuclease Activity |
title_sort | vapd in xylella fastidiosa is a thermostable protein with ribonuclease activity |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4687846/ https://www.ncbi.nlm.nih.gov/pubmed/26694028 http://dx.doi.org/10.1371/journal.pone.0145765 |
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