Proteomic analysis reveals suppression of bark chitinases and proteinase inhibitors in citrus plants affected by the citrus sudden death disease

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dc.contributor.authorCantu, M. D.
dc.contributor.authorMariano, A. G.
dc.contributor.authorPalma, Mario Sergio [UNESP]
dc.contributor.authorCarrilho, E.
dc.contributor.authorWulff, N. A.
dc.contributor.institutionFundo de Defesa da Citricultura (FUNDECITRUS)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T13:54:58Z
dc.date.available2014-05-20T13:54:58Z
dc.date.issued2008-10-01
dc.description.abstractCitrus sudden death (CSD) is a disease of unknown etiology that greatly affects sweet oranges grafted on Rangpur lime rootstock, the most important rootstock in Brazilian citriculture. We performed a proteomic analysis to generate information related to this plant pathogen interaction. Protein profiles from healthy, CSD-affected and CSD-tolerant stem barks, were generated using two-dimensional gel electrophoresis. The protein spots were well distributed over a pI range of 3.26 to 9.97 and a molecular weight (MW) range from 7.1 to 120 kDa. The patterns of expressed proteins on 2-DE gels made it possible to distinguish healthy barks from CSD-affected barks. Protein spots with MW around 30 kDa and pI values ranging from 4.5 to 5.2 were down-regulated in the CSD-affected rootstock bark. This set of protein spots was identified as chitinases. Another set of proteins, ranging in pI from 6.1 to 9.6 with an MW of about 20 kDa, were also suppressed in CSD-affected rootstock bark; these were identified as miraculin-like proteins, potential trypsin inhibitors. Downregulation of chitinases and proteinase inhibitors in CSD-affected plants is relevant since chitinases are well-known pathogenesis-related protein, and their activity against plant pathogens is largely accepted.en
dc.description.affiliationFundo Defesa Citricultura, Araraquara, SP, Brazil
dc.description.affiliationUniv São Paulo, Inst Quim São Carlos, São Carlos, SP, Brazil
dc.description.affiliationUniv Estadual Paulista, Inst Biociencias Rio Claro, Rio Claro, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Inst Biociencias Rio Claro, Rio Claro, SP, Brazil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.format.extent1084-1092
dc.identifierhttp://dx.doi.org/10.1094/PHYTO-98-10-1084
dc.identifier.citationPhytopathology. St Paul: Amer Phytopathological Soc, v. 98, n. 10, p. 1084-1092, 2008.
dc.identifier.doi10.1094/PHYTO-98-10-1084
dc.identifier.issn0031-949X
dc.identifier.lattes2901888624506535
dc.identifier.urihttp://hdl.handle.net/11449/19667
dc.identifier.wosWOS:000259345400005
dc.language.isoeng
dc.publisherAmer Phytopathological Soc
dc.relation.ispartofPhytopathology
dc.relation.ispartofjcr3.036
dc.rights.accessRightsAcesso aberto
dc.sourceWeb of Science
dc.subjectPlant proteomicsen
dc.titleProteomic analysis reveals suppression of bark chitinases and proteinase inhibitors in citrus plants affected by the citrus sudden death diseaseen
dc.typeArtigo
dcterms.rightsHolderAmer Phytopathological Soc
unesp.author.lattes2901888624506535
unesp.author.orcid0000-0001-7351-8220[4]
unesp.author.orcid0000-0002-4557-2075[5]
unesp.author.orcid0000-0002-7363-8211[3]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências, Rio Claropt

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Artigos - Biologia - IBRC