Antimicrobial activity of glycosidase inhibitory protein isolated from Cyphomandra betacea Sendt. fruit

Autores
Ordóñez, Roxana Mabel; Ordóñez, Adriana; Sayago, Jorge Esteban; Nieva Moreno, María Inés; Isla, Maria Ines
Año de publicación
2006
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Broad-spectrum antimicrobial activity of an invertase inhibitory protein (IIP) isolated from Cyphomandra betacea ripe fruits is documented. Minimal inhibitory concentration (MIC) values were determined by agar macrodilution and broth microdilution assays. This IIP inhibited the growth of xylophagous and phytopatogenic fungi (Ganoderma applanatum, Schizophyllum commune, Lenzites elegans, Pycnoporus sanguineous, Penicillium notatum, Aspergillus niger, Phomopsis sojae and Fusarium mango) and phytopathogenic bacteria (Xanthomonas campestris pvar vesicatoria CECT 792, Pseudomonas solanacearum CECT 125, Pseudomonas corrugata CECT 124, Pseudomonas syringae pv. syringae and Erwinia carotovora var carotovora). The IIP concentration required to completely inhibit the growth of all studied fungi ranged from 7.8 to 62.5 μg/ml. Phytopatogenic bacteria were the most sensitive, with MIC values between 7.8 and 31.25 μg/ml. Antifungal and antibacterial activities can be associated with their ability to inhibit hydrolytic enzymes. Our results indicate the possible participation of IIP in the plant defense mechanism and its potential application as a biocontrol agent against phytopathogenic fungi and bacteria. © 2005 Elsevier Inc. All rights reserved.
Fil: Ordóñez, Roxana Mabel. Universidad Nacional de Tucumán; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
Fil: Ordóñez, Adriana. Universidad Nacional de Tucumán; Argentina
Fil: Sayago, Jorge Esteban. Universidad Nacional de Tucumán; Argentina
Fil: Nieva Moreno, María Inés. Universidad Nacional de Tucumán; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química Biológica; Argentina
Fil: Isla, Maria Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina. Universidad Nacional de Tucumán; Argentina
Materia
ANTIBACTERIAL ACTIVITY
ANTIFUNGAL ACTIVITY
CYPHOMANDRA BETACEA SENDT. FRUIT
GLYCOSIDASES INHIBITORY PROTEIN
PATHOGENESIS RELATED PROTEIN
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/99814
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/99814
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Antimicrobial activity of glycosidase inhibitory protein isolated from Cyphomandra betacea Sendt. fruitOrdóñez, Roxana MabelOrdóñez, AdrianaSayago, Jorge EstebanNieva Moreno, María InésIsla, Maria InesANTIBACTERIAL ACTIVITYANTIFUNGAL ACTIVITYCYPHOMANDRA BETACEA SENDT. FRUITGLYCOSIDASES INHIBITORY PROTEINPATHOGENESIS RELATED PROTEINhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Broad-spectrum antimicrobial activity of an invertase inhibitory protein (IIP) isolated from Cyphomandra betacea ripe fruits is documented. Minimal inhibitory concentration (MIC) values were determined by agar macrodilution and broth microdilution assays. This IIP inhibited the growth of xylophagous and phytopatogenic fungi (Ganoderma applanatum, Schizophyllum commune, Lenzites elegans, Pycnoporus sanguineous, Penicillium notatum, Aspergillus niger, Phomopsis sojae and Fusarium mango) and phytopathogenic bacteria (Xanthomonas campestris pvar vesicatoria CECT 792, Pseudomonas solanacearum CECT 125, Pseudomonas corrugata CECT 124, Pseudomonas syringae pv. syringae and Erwinia carotovora var carotovora). The IIP concentration required to completely inhibit the growth of all studied fungi ranged from 7.8 to 62.5 μg/ml. Phytopatogenic bacteria were the most sensitive, with MIC values between 7.8 and 31.25 μg/ml. Antifungal and antibacterial activities can be associated with their ability to inhibit hydrolytic enzymes. Our results indicate the possible participation of IIP in the plant defense mechanism and its potential application as a biocontrol agent against phytopathogenic fungi and bacteria. © 2005 Elsevier Inc. All rights reserved.Fil: Ordóñez, Roxana Mabel. Universidad Nacional de Tucumán; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; ArgentinaFil: Ordóñez, Adriana. Universidad Nacional de Tucumán; ArgentinaFil: Sayago, Jorge Esteban. Universidad Nacional de Tucumán; ArgentinaFil: Nieva Moreno, María Inés. Universidad Nacional de Tucumán; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química Biológica; ArgentinaFil: Isla, Maria Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina. Universidad Nacional de Tucumán; ArgentinaElsevier Science Inc2006-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/99814Ordóñez, Roxana Mabel; Ordóñez, Adriana; Sayago, Jorge Esteban; Nieva Moreno, María Inés; Isla, Maria Ines; Antimicrobial activity of glycosidase inhibitory protein isolated from Cyphomandra betacea Sendt. fruit; Elsevier Science Inc; Peptides; 27; 6; 6-2006; 1187-11910196-9781CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.peptides.2005.11.016info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0196978105005632?via%3Dihubinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:59:32Zoai:ri.conicet.gov.ar:11336/99814instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:59:32.678CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Antimicrobial activity of glycosidase inhibitory protein isolated from Cyphomandra betacea Sendt. fruit
title Antimicrobial activity of glycosidase inhibitory protein isolated from Cyphomandra betacea Sendt. fruit
spellingShingle Antimicrobial activity of glycosidase inhibitory protein isolated from Cyphomandra betacea Sendt. fruit
Ordóñez, Roxana Mabel
ANTIBACTERIAL ACTIVITY
ANTIFUNGAL ACTIVITY
CYPHOMANDRA BETACEA SENDT. FRUIT
GLYCOSIDASES INHIBITORY PROTEIN
PATHOGENESIS RELATED PROTEIN
title_short Antimicrobial activity of glycosidase inhibitory protein isolated from Cyphomandra betacea Sendt. fruit
title_full Antimicrobial activity of glycosidase inhibitory protein isolated from Cyphomandra betacea Sendt. fruit
title_fullStr Antimicrobial activity of glycosidase inhibitory protein isolated from Cyphomandra betacea Sendt. fruit
title_full_unstemmed Antimicrobial activity of glycosidase inhibitory protein isolated from Cyphomandra betacea Sendt. fruit
title_sort Antimicrobial activity of glycosidase inhibitory protein isolated from Cyphomandra betacea Sendt. fruit
dc.creator.none.fl_str_mv Ordóñez, Roxana Mabel
Ordóñez, Adriana
Sayago, Jorge Esteban
Nieva Moreno, María Inés
Isla, Maria Ines
author Ordóñez, Roxana Mabel
author_facet Ordóñez, Roxana Mabel
Ordóñez, Adriana
Sayago, Jorge Esteban
Nieva Moreno, María Inés
Isla, Maria Ines
author_role author
author2 Ordóñez, Adriana
Sayago, Jorge Esteban
Nieva Moreno, María Inés
Isla, Maria Ines
author2_role author
author
author
author
dc.subject.none.fl_str_mv ANTIBACTERIAL ACTIVITY
ANTIFUNGAL ACTIVITY
CYPHOMANDRA BETACEA SENDT. FRUIT
GLYCOSIDASES INHIBITORY PROTEIN
PATHOGENESIS RELATED PROTEIN
topic ANTIBACTERIAL ACTIVITY
ANTIFUNGAL ACTIVITY
CYPHOMANDRA BETACEA SENDT. FRUIT
GLYCOSIDASES INHIBITORY PROTEIN
PATHOGENESIS RELATED PROTEIN
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Broad-spectrum antimicrobial activity of an invertase inhibitory protein (IIP) isolated from Cyphomandra betacea ripe fruits is documented. Minimal inhibitory concentration (MIC) values were determined by agar macrodilution and broth microdilution assays. This IIP inhibited the growth of xylophagous and phytopatogenic fungi (Ganoderma applanatum, Schizophyllum commune, Lenzites elegans, Pycnoporus sanguineous, Penicillium notatum, Aspergillus niger, Phomopsis sojae and Fusarium mango) and phytopathogenic bacteria (Xanthomonas campestris pvar vesicatoria CECT 792, Pseudomonas solanacearum CECT 125, Pseudomonas corrugata CECT 124, Pseudomonas syringae pv. syringae and Erwinia carotovora var carotovora). The IIP concentration required to completely inhibit the growth of all studied fungi ranged from 7.8 to 62.5 μg/ml. Phytopatogenic bacteria were the most sensitive, with MIC values between 7.8 and 31.25 μg/ml. Antifungal and antibacterial activities can be associated with their ability to inhibit hydrolytic enzymes. Our results indicate the possible participation of IIP in the plant defense mechanism and its potential application as a biocontrol agent against phytopathogenic fungi and bacteria. © 2005 Elsevier Inc. All rights reserved.
Fil: Ordóñez, Roxana Mabel. Universidad Nacional de Tucumán; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
Fil: Ordóñez, Adriana. Universidad Nacional de Tucumán; Argentina
Fil: Sayago, Jorge Esteban. Universidad Nacional de Tucumán; Argentina
Fil: Nieva Moreno, María Inés. Universidad Nacional de Tucumán; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química Biológica; Argentina
Fil: Isla, Maria Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina. Universidad Nacional de Tucumán; Argentina
description Broad-spectrum antimicrobial activity of an invertase inhibitory protein (IIP) isolated from Cyphomandra betacea ripe fruits is documented. Minimal inhibitory concentration (MIC) values were determined by agar macrodilution and broth microdilution assays. This IIP inhibited the growth of xylophagous and phytopatogenic fungi (Ganoderma applanatum, Schizophyllum commune, Lenzites elegans, Pycnoporus sanguineous, Penicillium notatum, Aspergillus niger, Phomopsis sojae and Fusarium mango) and phytopathogenic bacteria (Xanthomonas campestris pvar vesicatoria CECT 792, Pseudomonas solanacearum CECT 125, Pseudomonas corrugata CECT 124, Pseudomonas syringae pv. syringae and Erwinia carotovora var carotovora). The IIP concentration required to completely inhibit the growth of all studied fungi ranged from 7.8 to 62.5 μg/ml. Phytopatogenic bacteria were the most sensitive, with MIC values between 7.8 and 31.25 μg/ml. Antifungal and antibacterial activities can be associated with their ability to inhibit hydrolytic enzymes. Our results indicate the possible participation of IIP in the plant defense mechanism and its potential application as a biocontrol agent against phytopathogenic fungi and bacteria. © 2005 Elsevier Inc. All rights reserved.
publishDate 2006
dc.date.none.fl_str_mv 2006-06
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 http://hdl.handle.net/11336/99814
Ordóñez, Roxana Mabel; Ordóñez, Adriana; Sayago, Jorge Esteban; Nieva Moreno, María Inés; Isla, Maria Ines; Antimicrobial activity of glycosidase inhibitory protein isolated from Cyphomandra betacea Sendt. fruit; Elsevier Science Inc; Peptides; 27; 6; 6-2006; 1187-1191
0196-9781
CONICET Digital
CONICET
url http://hdl.handle.net/11336/99814
identifier_str_mv Ordóñez, Roxana Mabel; Ordóñez, Adriana; Sayago, Jorge Esteban; Nieva Moreno, María Inés; Isla, Maria Ines; Antimicrobial activity of glycosidase inhibitory protein isolated from Cyphomandra betacea Sendt. fruit; Elsevier Science Inc; Peptides; 27; 6; 6-2006; 1187-1191
0196-9781
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.peptides.2005.11.016
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0196978105005632?via%3Dihub
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science Inc
publisher.none.fl_str_mv Elsevier Science Inc
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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