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Abstract
Significant efforts are being made to minimize aflatoxin contamination in peanut seeds and one possible strategy is to understand and exploit the mechanisms of plant defense against fungal infection. In this study we have identified and characterized, at biochemical and molecular levels, plant protease inhibitors (PPIs) produced in peanut seeds of the resistant PI 337394 and the susceptible Forman cultivar during Aspergillus parasiticus colonization. With [ver mas...]
dc.contributor.authorMuller, Virginia
dc.contributor.authorBonacci, Gustavo Roberto
dc.contributor.authorBatthyany, Carlos
dc.contributor.authorAmé, María Valeria
dc.contributor.authorCarrari, Fernando
dc.contributor.authorGieco, Jorge Omar
dc.contributor.authorAsis, Ramón
dc.date.accessioned2019-01-24T11:52:53Z
dc.date.available2019-01-24T11:52:53Z
dc.date.issued2017-04
dc.identifier.issn0031-949X
dc.identifier.issn1943-7684
dc.identifier.otherhttps://doi.org/10.1094/PHYTO-09-16-0346-R
dc.identifier.urihttps://apsjournals.apsnet.org/doi/pdf/10.1094/PHYTO-09-16-0346-R
dc.identifier.urihttp://hdl.handle.net/20.500.12123/4322
dc.description.abstractSignificant efforts are being made to minimize aflatoxin contamination in peanut seeds and one possible strategy is to understand and exploit the mechanisms of plant defense against fungal infection. In this study we have identified and characterized, at biochemical and molecular levels, plant protease inhibitors (PPIs) produced in peanut seeds of the resistant PI 337394 and the susceptible Forman cultivar during Aspergillus parasiticus colonization. With chromatographic methods and 2D-electrophoresis-mass spectrometry we have isolated and identified four variants of Bowman-Birk trypsin inhibitor (BBTI) and a novel Kunitz-type protease inhibitor (KPI) produced in response to A. parasiticus colonization. KPI was detected only in the resistant cultivar, while BBTI was produced in the resistant cultivar in a higher concentration than susceptible cultivar and with different isoforms. The kinetic expression of KPI and BBTI genes along with trypsin inhibitory activity was analyzed in both cultivars during infection. In the susceptible cultivar an early PPI activity response was associated with BBTI occurrence. Meanwhile, in the resistant cultivar a later response with a larger increase in PPI activity was associated with BBTI and KPI occurrence. The biological significance of PPI in seed defense against fungal infection was analyzed and linked to inhibitory properties on enzymes released by the fungus during infection, and to the antifungal effect of KPI.eng
dc.formatapplication/pdfes_AR
dc.language.isoenges_AR
dc.publisherAmerican Phytopathological Societyes_AR
dc.rightsinfo:eu-repo/semantics/openAccesses_AR
dc.sourcePhytopathology 107 (4) : 474-482 (April 2017)es_AR
dc.subjectArachis hypogaeaes_AR
dc.subjectSemillaes_AR
dc.subjectSeedseng
dc.subjectVariedadeses_AR
dc.subjectVarietieseng
dc.subjectResistencia a la Enfermedades_AR
dc.subjectDisease Resistanceeng
dc.subjectAspergillus parasiticuses_AR
dc.subjectInhibidores de Proteinasases_AR
dc.subjectProteinase Inhibitorseng
dc.subject.otherManíes_AR
dc.subject.otherInhibidores de Proteasases_AR
dc.subject.otherProtease Inhibitorseng
dc.titlePeanut seed cultivars with contrasting resistance to Aspergillus parasiticus colonization display differential temporal response of protease inhibitorses_AR
dc.typeinfo:ar-repo/semantics/artículoes_AR
dc.typeinfo:eu-repo/semantics/articlees_AR
dc.typeinfo:eu-repo/semantics/publishedVersiones_AR
dc.description.origenInstituto de Biotecnologíaes_AR
dc.description.filFil: Muller, Virginia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentinaes_AR
dc.description.filFil: Bonacci, Gustavo Roberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentinaes_AR
dc.description.filFil: Batthyany, Carlos. Institut Pasteur de Montevideo. Unidad de Bioquímica y Proteómica Analítica; Uruguayes_AR
dc.description.filFil: Amé, María Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentinaes_AR
dc.description.filFil: Carrari, Fernando Oscar. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentinaes_AR
dc.description.filFil: Gieco, Jorge Omar. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Manfredi; Argentinaes_AR
dc.description.filFil: Asis, Ramón. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentinaes_AR
dc.subtypecientifico


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