PLPKI: A novel serine protease inhibitor as a potential biochemical marker involved in horizontal resistance to Phytophthora infestans

Autores
Feldman, M.; Andreu, A.B.; Korgan, S.; Lobato, M.C.; Huarte, M.; Lee Walling, Linda; Daleo, Gustavo Raúl
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión enviada
Descripción
Potato leaves infected with Phytophthorainfestans produced a serine protease inhibitor (PLPKI) with specificity for microbial proteases. Sequencing of the first twenty residues at the NH2-terminus of the mature PLPKI polypeptide demonstrated that PLPKI is a novel member of the potato protease inhibitor I family. PLPKI inhibited the activity of extracellular proteases produced by two pathogens of potato, P.infestans and Rhizoctoniasolani, but was inactive against proteases secreted into the culture media by the binucleate Rhizoctonia N2, a non-pathogenic fungus for potato. Western blot analysis showed a positive correlation between the levels of PLPKI and the degree of horizontal resistance, showing its highest accumulation in clone OKA 5632.11, which has been described as highly resistant. This correlation, together with the ability of PLPKI to completely abolish the secreted serine protease activity of P.infestans, suggests that PLPKI may have an active role in protecting potato plants from this pathogenic oomycete and that it could be used as a suitable biochemical marker to help breeders in the selection of cultivars with high degree of horizontal resistance.
Materia
Bioquímica y Biología Molecular
plant defence
Potato
quantitative resistance
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-nd/4.0/
Repositorio
CIC Digital (CICBA)
Institución
Comisión de Investigaciones Científicas de la Provincia de Buenos Aires
OAI Identificador
oai:digital.cic.gba.gob.ar:11746/5524

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oai_identifier_str oai:digital.cic.gba.gob.ar:11746/5524
network_acronym_str CICBA
repository_id_str 9441
network_name_str CIC Digital (CICBA)
spelling PLPKI: A novel serine protease inhibitor as a potential biochemical marker involved in horizontal resistance to Phytophthora infestansFeldman, M.Andreu, A.B.Korgan, S.Lobato, M.C.Huarte, M.Lee Walling, LindaDaleo, Gustavo RaúlBioquímica y Biología Molecularplant defencePotatoquantitative resistancePotato leaves infected with <em>Phytophthorainfestans</em> produced a serine protease inhibitor (PLPKI) with specificity for microbial proteases. Sequencing of the first twenty residues at the NH2-terminus of the mature PLPKI polypeptide demonstrated that PLPKI is a novel member of the potato protease inhibitor I family. PLPKI inhibited the activity of extracellular proteases produced by two pathogens of potato, <em>P.infestans</em> and <em>Rhizoctoniasolani</em>, but was inactive against proteases secreted into the culture media by the binucleate <em>Rhizoctonia</em> N2, a non-pathogenic fungus for potato. Western blot analysis showed a positive correlation between the levels of PLPKI and the degree of horizontal resistance, showing its highest accumulation in clone OKA 5632.11, which has been described as highly resistant. This correlation, together with the ability of PLPKI to completely abolish the secreted serine protease activity of <em>P.infestans</em>, suggests that PLPKI may have an active role in protecting potato plants from this pathogenic oomycete and that it could be used as a suitable biochemical marker to help breeders in the selection of cultivars with high degree of horizontal resistance.2014-01-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/submittedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttps://digital.cic.gba.gob.ar/handle/11746/5524enginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-nd/4.0/reponame:CIC Digital (CICBA)instname:Comisión de Investigaciones Científicas de la Provincia de Buenos Airesinstacron:CICBA2025-09-04T09:43:16Zoai:digital.cic.gba.gob.ar:11746/5524Institucionalhttp://digital.cic.gba.gob.arOrganismo científico-tecnológicoNo correspondehttp://digital.cic.gba.gob.ar/oai/snrdmarisa.degiusti@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:94412025-09-04 09:43:17.281CIC Digital (CICBA) - Comisión de Investigaciones Científicas de la Provincia de Buenos Airesfalse
dc.title.none.fl_str_mv PLPKI: A novel serine protease inhibitor as a potential biochemical marker involved in horizontal resistance to Phytophthora infestans
title PLPKI: A novel serine protease inhibitor as a potential biochemical marker involved in horizontal resistance to Phytophthora infestans
spellingShingle PLPKI: A novel serine protease inhibitor as a potential biochemical marker involved in horizontal resistance to Phytophthora infestans
Feldman, M.
Bioquímica y Biología Molecular
plant defence
Potato
quantitative resistance
title_short PLPKI: A novel serine protease inhibitor as a potential biochemical marker involved in horizontal resistance to Phytophthora infestans
title_full PLPKI: A novel serine protease inhibitor as a potential biochemical marker involved in horizontal resistance to Phytophthora infestans
title_fullStr PLPKI: A novel serine protease inhibitor as a potential biochemical marker involved in horizontal resistance to Phytophthora infestans
title_full_unstemmed PLPKI: A novel serine protease inhibitor as a potential biochemical marker involved in horizontal resistance to Phytophthora infestans
title_sort PLPKI: A novel serine protease inhibitor as a potential biochemical marker involved in horizontal resistance to Phytophthora infestans
dc.creator.none.fl_str_mv Feldman, M.
Andreu, A.B.
Korgan, S.
Lobato, M.C.
Huarte, M.
Lee Walling, Linda
Daleo, Gustavo Raúl
author Feldman, M.
author_facet Feldman, M.
Andreu, A.B.
Korgan, S.
Lobato, M.C.
Huarte, M.
Lee Walling, Linda
Daleo, Gustavo Raúl
author_role author
author2 Andreu, A.B.
Korgan, S.
Lobato, M.C.
Huarte, M.
Lee Walling, Linda
Daleo, Gustavo Raúl
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Bioquímica y Biología Molecular
plant defence
Potato
quantitative resistance
topic Bioquímica y Biología Molecular
plant defence
Potato
quantitative resistance
dc.description.none.fl_txt_mv Potato leaves infected with <em>Phytophthorainfestans</em> produced a serine protease inhibitor (PLPKI) with specificity for microbial proteases. Sequencing of the first twenty residues at the NH2-terminus of the mature PLPKI polypeptide demonstrated that PLPKI is a novel member of the potato protease inhibitor I family. PLPKI inhibited the activity of extracellular proteases produced by two pathogens of potato, <em>P.infestans</em> and <em>Rhizoctoniasolani</em>, but was inactive against proteases secreted into the culture media by the binucleate <em>Rhizoctonia</em> N2, a non-pathogenic fungus for potato. Western blot analysis showed a positive correlation between the levels of PLPKI and the degree of horizontal resistance, showing its highest accumulation in clone OKA 5632.11, which has been described as highly resistant. This correlation, together with the ability of PLPKI to completely abolish the secreted serine protease activity of <em>P.infestans</em>, suggests that PLPKI may have an active role in protecting potato plants from this pathogenic oomycete and that it could be used as a suitable biochemical marker to help breeders in the selection of cultivars with high degree of horizontal resistance.
description Potato leaves infected with <em>Phytophthorainfestans</em> produced a serine protease inhibitor (PLPKI) with specificity for microbial proteases. Sequencing of the first twenty residues at the NH2-terminus of the mature PLPKI polypeptide demonstrated that PLPKI is a novel member of the potato protease inhibitor I family. PLPKI inhibited the activity of extracellular proteases produced by two pathogens of potato, <em>P.infestans</em> and <em>Rhizoctoniasolani</em>, but was inactive against proteases secreted into the culture media by the binucleate <em>Rhizoctonia</em> N2, a non-pathogenic fungus for potato. Western blot analysis showed a positive correlation between the levels of PLPKI and the degree of horizontal resistance, showing its highest accumulation in clone OKA 5632.11, which has been described as highly resistant. This correlation, together with the ability of PLPKI to completely abolish the secreted serine protease activity of <em>P.infestans</em>, suggests that PLPKI may have an active role in protecting potato plants from this pathogenic oomycete and that it could be used as a suitable biochemical marker to help breeders in the selection of cultivars with high degree of horizontal resistance.
publishDate 2014
dc.date.none.fl_str_mv 2014-01-06
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/submittedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str submittedVersion
dc.identifier.none.fl_str_mv https://digital.cic.gba.gob.ar/handle/11746/5524
url https://digital.cic.gba.gob.ar/handle/11746/5524
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-nd/4.0/
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:CIC Digital (CICBA)
instname:Comisión de Investigaciones Científicas de la Provincia de Buenos Aires
instacron:CICBA
reponame_str CIC Digital (CICBA)
collection CIC Digital (CICBA)
instname_str Comisión de Investigaciones Científicas de la Provincia de Buenos Aires
instacron_str CICBA
institution CICBA
repository.name.fl_str_mv CIC Digital (CICBA) - Comisión de Investigaciones Científicas de la Provincia de Buenos Aires
repository.mail.fl_str_mv marisa.degiusti@sedici.unlp.edu.ar
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