Peanut seed cultivars with contrasting resistance to Aspergillus parasiticus colonization display differential temporal response of protease inhibitors

Autores
Muller, Virginia; Bonacci, Gustavo Roberto; Batthyany, Carlos; Amé, María Valeria; Carrari, Fernando; Gieco, Jorge Omar; Asis, Ramón
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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 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.
Instituto de Biotecnología
Fil: 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; Argentina
Fil: 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; Argentina
Fil: Batthyany, Carlos. Institut Pasteur de Montevideo. Unidad de Bioquímica y Proteómica Analítica; Uruguay
Fil: 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; Argentina
Fil: Carrari, Fernando Oscar. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
Fil: Gieco, Jorge Omar. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Manfredi; Argentina
Fil: 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; Argentina
Fuente
Phytopathology 107 (4) : 474-482 (April 2017)
Materia
Arachis hypogaea
Semilla
Variedades
Resistencia a la Enfermedad
Aspergillus parasiticus
Inhibidores de Proteinasas
Seeds
Varieties
Disease Resistance
Proteinase Inhibitors
Maní
Inhibidores de Proteasas
Protease Inhibitors
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
INTA Digital (INTA)
Institución
Instituto Nacional de Tecnología Agropecuaria
OAI Identificador
oai:localhost:20.500.12123/4322
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oai_identifier_str oai:localhost:20.500.12123/4322
network_acronym_str INTADig
repository_id_str l
network_name_str INTA Digital (INTA)
spelling Peanut seed cultivars with contrasting resistance to Aspergillus parasiticus colonization display differential temporal response of protease inhibitorsMuller, VirginiaBonacci, Gustavo RobertoBatthyany, CarlosAmé, María ValeriaCarrari, FernandoGieco, Jorge OmarAsis, RamónArachis hypogaeaSemillaVariedadesResistencia a la EnfermedadAspergillus parasiticusInhibidores de ProteinasasSeedsVarietiesDisease ResistanceProteinase InhibitorsManíInhibidores de ProteasasProtease InhibitorsSignificant 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.Instituto de BiotecnologíaFil: 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; ArgentinaFil: 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; ArgentinaFil: Batthyany, Carlos. Institut Pasteur de Montevideo. Unidad de Bioquímica y Proteómica Analítica; UruguayFil: 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; ArgentinaFil: Carrari, Fernando Oscar. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; ArgentinaFil: Gieco, Jorge Omar. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Manfredi; ArgentinaFil: 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; ArgentinaAmerican Phytopathological Society2019-01-24T11:52:53Z2019-01-24T11:52:53Z2017-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttps://apsjournals.apsnet.org/doi/pdf/10.1094/PHYTO-09-16-0346-Rhttp://hdl.handle.net/20.500.12123/43220031-949X1943-7684https://doi.org/10.1094/PHYTO-09-16-0346-RPhytopathology 107 (4) : 474-482 (April 2017)reponame:INTA Digital (INTA)instname:Instituto Nacional de Tecnología Agropecuariaenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)2025-09-29T13:44:33Zoai:localhost:20.500.12123/4322instacron:INTAInstitucionalhttp://repositorio.inta.gob.ar/Organismo científico-tecnológicoNo correspondehttp://repositorio.inta.gob.ar/oai/requesttripaldi.nicolas@inta.gob.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:l2025-09-29 13:44:34.1INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuariafalse
dc.title.none.fl_str_mv Peanut seed cultivars with contrasting resistance to Aspergillus parasiticus colonization display differential temporal response of protease inhibitors
title Peanut seed cultivars with contrasting resistance to Aspergillus parasiticus colonization display differential temporal response of protease inhibitors
spellingShingle Peanut seed cultivars with contrasting resistance to Aspergillus parasiticus colonization display differential temporal response of protease inhibitors
Muller, Virginia
Arachis hypogaea
Semilla
Variedades
Resistencia a la Enfermedad
Aspergillus parasiticus
Inhibidores de Proteinasas
Seeds
Varieties
Disease Resistance
Proteinase Inhibitors
Maní
Inhibidores de Proteasas
Protease Inhibitors
title_short Peanut seed cultivars with contrasting resistance to Aspergillus parasiticus colonization display differential temporal response of protease inhibitors
title_full Peanut seed cultivars with contrasting resistance to Aspergillus parasiticus colonization display differential temporal response of protease inhibitors
title_fullStr Peanut seed cultivars with contrasting resistance to Aspergillus parasiticus colonization display differential temporal response of protease inhibitors
title_full_unstemmed Peanut seed cultivars with contrasting resistance to Aspergillus parasiticus colonization display differential temporal response of protease inhibitors
title_sort Peanut seed cultivars with contrasting resistance to Aspergillus parasiticus colonization display differential temporal response of protease inhibitors
dc.creator.none.fl_str_mv Muller, Virginia
Bonacci, Gustavo Roberto
Batthyany, Carlos
Amé, María Valeria
Carrari, Fernando
Gieco, Jorge Omar
Asis, Ramón
author Muller, Virginia
author_facet Muller, Virginia
Bonacci, Gustavo Roberto
Batthyany, Carlos
Amé, María Valeria
Carrari, Fernando
Gieco, Jorge Omar
Asis, Ramón
author_role author
author2 Bonacci, Gustavo Roberto
Batthyany, Carlos
Amé, María Valeria
Carrari, Fernando
Gieco, Jorge Omar
Asis, Ramón
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Arachis hypogaea
Semilla
Variedades
Resistencia a la Enfermedad
Aspergillus parasiticus
Inhibidores de Proteinasas
Seeds
Varieties
Disease Resistance
Proteinase Inhibitors
Maní
Inhibidores de Proteasas
Protease Inhibitors
topic Arachis hypogaea
Semilla
Variedades
Resistencia a la Enfermedad
Aspergillus parasiticus
Inhibidores de Proteinasas
Seeds
Varieties
Disease Resistance
Proteinase Inhibitors
Maní
Inhibidores de Proteasas
Protease Inhibitors
dc.description.none.fl_txt_mv 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 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.
Instituto de Biotecnología
Fil: 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; Argentina
Fil: 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; Argentina
Fil: Batthyany, Carlos. Institut Pasteur de Montevideo. Unidad de Bioquímica y Proteómica Analítica; Uruguay
Fil: 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; Argentina
Fil: Carrari, Fernando Oscar. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
Fil: Gieco, Jorge Omar. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Manfredi; Argentina
Fil: 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; Argentina
description 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 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.
publishDate 2017
dc.date.none.fl_str_mv 2017-04
2019-01-24T11:52:53Z
2019-01-24T11:52:53Z
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://apsjournals.apsnet.org/doi/pdf/10.1094/PHYTO-09-16-0346-R
http://hdl.handle.net/20.500.12123/4322
0031-949X
1943-7684
https://doi.org/10.1094/PHYTO-09-16-0346-R
url https://apsjournals.apsnet.org/doi/pdf/10.1094/PHYTO-09-16-0346-R
http://hdl.handle.net/20.500.12123/4322
https://doi.org/10.1094/PHYTO-09-16-0346-R
identifier_str_mv 0031-949X
1943-7684
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv American Phytopathological Society
publisher.none.fl_str_mv American Phytopathological Society
dc.source.none.fl_str_mv Phytopathology 107 (4) : 474-482 (April 2017)
reponame:INTA Digital (INTA)
instname:Instituto Nacional de Tecnología Agropecuaria
reponame_str INTA Digital (INTA)
collection INTA Digital (INTA)
instname_str Instituto Nacional de Tecnología Agropecuaria
repository.name.fl_str_mv INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuaria
repository.mail.fl_str_mv tripaldi.nicolas@inta.gob.ar
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score 12.558318

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