Proteomics-based identification of differentially abundant proteins reveals adaptation mechanisms of Xanthomonas citri subsp. citri during Citrus sinensis infection

Detalhes bibliográficos
Autor(a) principal: Moreira, Leandro M.
Data de Publicação: 2017
Outros Autores: Soares, Márcia R., Facincani, Agda P. [UNESP], Ferreira, Cristiano B. [UNESP], Ferreira, Rafael M. [UNESP], Ferro, Maria I. T. [UNESP], Gozzo, Fábio C., Felestrino, Érica B., Assis, Renata A. B., Garcia, Camila Carrião M., Setubal, João C., Ferro, Jesus A. [UNESP], De Oliveira, Julio C.F.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1186/s12866-017-1063-x
http://hdl.handle.net/11449/174874
Resumo: Background: Xanthomonas citri subsp. citri (Xac) is the causal agent of citrus canker. A proteomic analysis under in planta infectious and non-infectious conditions was conducted in order to increase our knowledge about the adaptive process of Xac during infection. Results: For that, a 2D-based proteomic analysis of Xac at 1, 3 and 5 days after inoculation, in comparison to Xac growth in NB media was carried out and followed by MALDI-TOF-TOF identification of 124 unique differentially abundant proteins. Among them, 79 correspond to up-regulated proteins in at least one of the three stages of infection. Our results indicate an important role of proteins related to biofilm synthesis, lipopolysaccharides biosynthesis, and iron uptake and metabolism as possible modulators of plant innate immunity, and revealed an intricate network of proteins involved in reactive oxygen species adaptation during Plants' Oxidative Burst response. We also identified proteins previously unknown to be involved in Xac-Citrus interaction, including the hypothetical protein XAC3981. A mutant strain for this gene has proved to be non-pathogenic in respect to classical symptoms of citrus canker induced in compatible plants. Conclusions: This is the first time that a protein repertoire is shown to be active and working in an integrated manner during the infection process in a compatible host, pointing to an elaborate mechanism for adaptation of Xac once inside the plant.
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spelling Proteomics-based identification of differentially abundant proteins reveals adaptation mechanisms of Xanthomonas citri subsp. citri during Citrus sinensis infectionBiofilmIron uptake and metabolismLPS modulationPlants'Oxidative burstXanthomonas, adaptation mechanismsBackground: Xanthomonas citri subsp. citri (Xac) is the causal agent of citrus canker. A proteomic analysis under in planta infectious and non-infectious conditions was conducted in order to increase our knowledge about the adaptive process of Xac during infection. Results: For that, a 2D-based proteomic analysis of Xac at 1, 3 and 5 days after inoculation, in comparison to Xac growth in NB media was carried out and followed by MALDI-TOF-TOF identification of 124 unique differentially abundant proteins. Among them, 79 correspond to up-regulated proteins in at least one of the three stages of infection. Our results indicate an important role of proteins related to biofilm synthesis, lipopolysaccharides biosynthesis, and iron uptake and metabolism as possible modulators of plant innate immunity, and revealed an intricate network of proteins involved in reactive oxygen species adaptation during Plants' Oxidative Burst response. We also identified proteins previously unknown to be involved in Xac-Citrus interaction, including the hypothetical protein XAC3981. A mutant strain for this gene has proved to be non-pathogenic in respect to classical symptoms of citrus canker induced in compatible plants. Conclusions: This is the first time that a protein repertoire is shown to be active and working in an integrated manner during the infection process in a compatible host, pointing to an elaborate mechanism for adaptation of Xac once inside the plant.Departamento de Ciências Biológicas (DECBI) Instituto de Ciências Exatas e Biológicas (ICEB) Universidade Federal de Ouro Preto (UFOP)Núcleo de Pesquisas em Ciências Biológicas (NUPEB) Universidade Federal de Ouro PretoDepartamento de Bioquímica (DBq) Instituto de Química (IQ) Universidade Federal Do Rio de Janeiro (UFRJ)Faculdade de Ciências Agrárias e Veterinárias de Jaboticabal UNESP - Universidade Estadual Paulista Departamento de TecnologiaInstituto de Química Universidade Estadual de Campinas (UNICAMP)Departamento de Bioquímica (DB) Instituto de Química (IQ) Universidade de São Paulo (USP)Departamento de Ciências Biológicas (DCB) Universidade Federal de São Paulo (UNIFESP)Biocomplexity Institute Virginia TechFaculdade de Ciências Agrárias e Veterinárias de Jaboticabal UNESP - Universidade Estadual Paulista Departamento de TecnologiaUniversidade Federal de Ouro Preto (UFOP)Universidade Federal de Ouro PretoUniversidade Federal do Rio de Janeiro (UFRJ)Universidade Estadual Paulista (Unesp)Universidade Estadual de Campinas (UNICAMP)Universidade de São Paulo (USP)Universidade Federal de São Paulo (UNIFESP)Virginia TechMoreira, Leandro M.Soares, Márcia R.Facincani, Agda P. [UNESP]Ferreira, Cristiano B. [UNESP]Ferreira, Rafael M. [UNESP]Ferro, Maria I. T. [UNESP]Gozzo, Fábio C.Felestrino, Érica B.Assis, Renata A. B.Garcia, Camila Carrião M.Setubal, João C.Ferro, Jesus A. [UNESP]De Oliveira, Julio C.F.2018-12-11T17:13:15Z2018-12-11T17:13:15Z2017-07-11info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://dx.doi.org/10.1186/s12866-017-1063-xBMC Microbiology, v. 17, n. 1, 2017.1471-2180http://hdl.handle.net/11449/17487410.1186/s12866-017-1063-x2-s2.0-850222245252-s2.0-85022224525.pdfScopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengBMC Microbiology1,242info:eu-repo/semantics/openAccess2023-12-25T06:22:37Zoai:repositorio.unesp.br:11449/174874Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462023-12-25T06:22:37Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Proteomics-based identification of differentially abundant proteins reveals adaptation mechanisms of Xanthomonas citri subsp. citri during Citrus sinensis infection
title Proteomics-based identification of differentially abundant proteins reveals adaptation mechanisms of Xanthomonas citri subsp. citri during Citrus sinensis infection
spellingShingle Proteomics-based identification of differentially abundant proteins reveals adaptation mechanisms of Xanthomonas citri subsp. citri during Citrus sinensis infection
Moreira, Leandro M.
Biofilm
Iron uptake and metabolism
LPS modulation
Plants'Oxidative burst
Xanthomonas, adaptation mechanisms
title_short Proteomics-based identification of differentially abundant proteins reveals adaptation mechanisms of Xanthomonas citri subsp. citri during Citrus sinensis infection
title_full Proteomics-based identification of differentially abundant proteins reveals adaptation mechanisms of Xanthomonas citri subsp. citri during Citrus sinensis infection
title_fullStr Proteomics-based identification of differentially abundant proteins reveals adaptation mechanisms of Xanthomonas citri subsp. citri during Citrus sinensis infection
title_full_unstemmed Proteomics-based identification of differentially abundant proteins reveals adaptation mechanisms of Xanthomonas citri subsp. citri during Citrus sinensis infection
title_sort Proteomics-based identification of differentially abundant proteins reveals adaptation mechanisms of Xanthomonas citri subsp. citri during Citrus sinensis infection
author Moreira, Leandro M.
author_facet Moreira, Leandro M.
Soares, Márcia R.
Facincani, Agda P. [UNESP]
Ferreira, Cristiano B. [UNESP]
Ferreira, Rafael M. [UNESP]
Ferro, Maria I. T. [UNESP]
Gozzo, Fábio C.
Felestrino, Érica B.
Assis, Renata A. B.
Garcia, Camila Carrião M.
Setubal, João C.
Ferro, Jesus A. [UNESP]
De Oliveira, Julio C.F.
author_role author
author2 Soares, Márcia R.
Facincani, Agda P. [UNESP]
Ferreira, Cristiano B. [UNESP]
Ferreira, Rafael M. [UNESP]
Ferro, Maria I. T. [UNESP]
Gozzo, Fábio C.
Felestrino, Érica B.
Assis, Renata A. B.
Garcia, Camila Carrião M.
Setubal, João C.
Ferro, Jesus A. [UNESP]
De Oliveira, Julio C.F.
author2_role author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Federal de Ouro Preto (UFOP)
Universidade Federal de Ouro Preto
Universidade Federal do Rio de Janeiro (UFRJ)
Universidade Estadual Paulista (Unesp)
Universidade Estadual de Campinas (UNICAMP)
Universidade de São Paulo (USP)
Universidade Federal de São Paulo (UNIFESP)
Virginia Tech
dc.contributor.author.fl_str_mv Moreira, Leandro M.
Soares, Márcia R.
Facincani, Agda P. [UNESP]
Ferreira, Cristiano B. [UNESP]
Ferreira, Rafael M. [UNESP]
Ferro, Maria I. T. [UNESP]
Gozzo, Fábio C.
Felestrino, Érica B.
Assis, Renata A. B.
Garcia, Camila Carrião M.
Setubal, João C.
Ferro, Jesus A. [UNESP]
De Oliveira, Julio C.F.
dc.subject.por.fl_str_mv Biofilm
Iron uptake and metabolism
LPS modulation
Plants'Oxidative burst
Xanthomonas, adaptation mechanisms
topic Biofilm
Iron uptake and metabolism
LPS modulation
Plants'Oxidative burst
Xanthomonas, adaptation mechanisms
description Background: Xanthomonas citri subsp. citri (Xac) is the causal agent of citrus canker. A proteomic analysis under in planta infectious and non-infectious conditions was conducted in order to increase our knowledge about the adaptive process of Xac during infection. Results: For that, a 2D-based proteomic analysis of Xac at 1, 3 and 5 days after inoculation, in comparison to Xac growth in NB media was carried out and followed by MALDI-TOF-TOF identification of 124 unique differentially abundant proteins. Among them, 79 correspond to up-regulated proteins in at least one of the three stages of infection. Our results indicate an important role of proteins related to biofilm synthesis, lipopolysaccharides biosynthesis, and iron uptake and metabolism as possible modulators of plant innate immunity, and revealed an intricate network of proteins involved in reactive oxygen species adaptation during Plants' Oxidative Burst response. We also identified proteins previously unknown to be involved in Xac-Citrus interaction, including the hypothetical protein XAC3981. A mutant strain for this gene has proved to be non-pathogenic in respect to classical symptoms of citrus canker induced in compatible plants. Conclusions: This is the first time that a protein repertoire is shown to be active and working in an integrated manner during the infection process in a compatible host, pointing to an elaborate mechanism for adaptation of Xac once inside the plant.
publishDate 2017
dc.date.none.fl_str_mv 2017-07-11
2018-12-11T17:13:15Z
2018-12-11T17:13:15Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1186/s12866-017-1063-x
BMC Microbiology, v. 17, n. 1, 2017.
1471-2180
http://hdl.handle.net/11449/174874
10.1186/s12866-017-1063-x
2-s2.0-85022224525
2-s2.0-85022224525.pdf
url http://dx.doi.org/10.1186/s12866-017-1063-x
http://hdl.handle.net/11449/174874
identifier_str_mv BMC Microbiology, v. 17, n. 1, 2017.
1471-2180
10.1186/s12866-017-1063-x
2-s2.0-85022224525
2-s2.0-85022224525.pdf
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv BMC Microbiology
1,242
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
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instname_str Universidade Estadual Paulista (UNESP)
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institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
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