Antimicrobial activity of an aspartic protease from Salpichroa origanifolia fruits

Autores
Díaz, María Eugenia; Rocha, Gabriela Fernanda; Kise, Francisco; Rosso, A. M.; Guevara, Maria Gabriela; Parisi, M.G.
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Abstract: Plant proteases play a fundamental role in several processes like growth, development and in response to biotic and abiotic stress. In particular, aspartic proteases (AP) are expressed in different plant organs and have antimicrobial activity. Previously, we purified an AP from Salpichroa origanifolia fruits called salpichroin. The aim of this work was to determine the cytotoxic activity of this enzyme on selected plant and human pathogens. For this purpose, the growth of the selected pathogens was analysed after exposure to different concentrations of salpichroin. The results showed that the enzyme was capable of inhibiting Fusarium solani and Staphylococcus aureus in a dose-dependent manner. It was determined that 1·2 μmol l−1 of salpichroin was necessary to inhibit 50% of conidial germination, and the minimal bactericidal concentration was between 1·9 and 2·5 μmol l−1. Using SYTOX Green dye we were able to demonstrate that salpichroin cause membrane permeabilization. Moreover, the enzyme treated with its specific inhibitor pepstatin A did not lose its antibacterial activity. This finding demonstrates that the cytotoxic activity of salpichroin is due to the alteration of the cell plasma membrane barrier but not due to its proteolytic activity. Antimicrobial activity of the AP could represent a potential alternative for the control of pathogens that affect humans or crops of economic interest. Significance and Impact of the Study: This study provides insights into the antimicrobial activity of an aspartic protease isolated from Salpichroa origanifolia fruits on plant and human pathogens. The proteinase inhibited Fusarium solani and Staphylococcus aureus in a dose-dependent manner due to the alteration of the cell plasma membrane barrier but not due to its proteolytic activity. Antimicrobial activity of salpichroin suggests its potential applications as an important tool for the control of pathogenic micro-organisms affecting humans and crops of economic interest. Therefore, it would represent a new alternative to avoid the problems of environmental pollution and antimicrobial resistance.
Fil: Díaz, María Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Luján; Argentina
Fil: Rocha, Gabriela Fernanda. Universidad Nacional de Luján; Argentina
Fil: Kise, Francisco. Universidad Nacional de Luján; Argentina
Fil: Rosso, A. M.. Universidad Nacional de Luján; Argentina
Fil: Guevara, Maria Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: Parisi, M.G.. Universidad Nacional de Luján; Argentina
Materia
antimicrobials
cytotoxicity
fungi
proteinase
Staphylococci
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:11336/87396
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/87396
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Antimicrobial activity of an aspartic protease from Salpichroa origanifolia fruitsDíaz, María EugeniaRocha, Gabriela FernandaKise, FranciscoRosso, A. M.Guevara, Maria GabrielaParisi, M.G.antimicrobialscytotoxicityfungiproteinaseStaphylococcihttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Abstract: Plant proteases play a fundamental role in several processes like growth, development and in response to biotic and abiotic stress. In particular, aspartic proteases (AP) are expressed in different plant organs and have antimicrobial activity. Previously, we purified an AP from Salpichroa origanifolia fruits called salpichroin. The aim of this work was to determine the cytotoxic activity of this enzyme on selected plant and human pathogens. For this purpose, the growth of the selected pathogens was analysed after exposure to different concentrations of salpichroin. The results showed that the enzyme was capable of inhibiting Fusarium solani and Staphylococcus aureus in a dose-dependent manner. It was determined that 1·2 μmol l−1 of salpichroin was necessary to inhibit 50% of conidial germination, and the minimal bactericidal concentration was between 1·9 and 2·5 μmol l−1. Using SYTOX Green dye we were able to demonstrate that salpichroin cause membrane permeabilization. Moreover, the enzyme treated with its specific inhibitor pepstatin A did not lose its antibacterial activity. This finding demonstrates that the cytotoxic activity of salpichroin is due to the alteration of the cell plasma membrane barrier but not due to its proteolytic activity. Antimicrobial activity of the AP could represent a potential alternative for the control of pathogens that affect humans or crops of economic interest. Significance and Impact of the Study: This study provides insights into the antimicrobial activity of an aspartic protease isolated from Salpichroa origanifolia fruits on plant and human pathogens. The proteinase inhibited Fusarium solani and Staphylococcus aureus in a dose-dependent manner due to the alteration of the cell plasma membrane barrier but not due to its proteolytic activity. Antimicrobial activity of salpichroin suggests its potential applications as an important tool for the control of pathogenic micro-organisms affecting humans and crops of economic interest. Therefore, it would represent a new alternative to avoid the problems of environmental pollution and antimicrobial resistance.Fil: Díaz, María Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Luján; ArgentinaFil: Rocha, Gabriela Fernanda. Universidad Nacional de Luján; ArgentinaFil: Kise, Francisco. Universidad Nacional de Luján; ArgentinaFil: Rosso, A. M.. Universidad Nacional de Luján; ArgentinaFil: Guevara, Maria Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; ArgentinaFil: Parisi, M.G.. Universidad Nacional de Luján; ArgentinaWiley Blackwell Publishing, Inc2018-04-24info: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/11336/87396Díaz, María Eugenia; Rocha, Gabriela Fernanda; Kise, Francisco; Rosso, A. M.; Guevara, Maria Gabriela; et al.; Antimicrobial activity of an aspartic protease from Salpichroa origanifolia fruits; Wiley Blackwell Publishing, Inc; Letters in Applied Microbiology; 67; 2; 24-4-2018; 168-1740266-8254CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pubmed/29740840info:eu-repo/semantics/altIdentifier/doi/10.1111/lam.13006info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:58:30Zoai:ri.conicet.gov.ar:11336/87396instacron: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 09:58:31.149CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Antimicrobial activity of an aspartic protease from Salpichroa origanifolia fruits
title Antimicrobial activity of an aspartic protease from Salpichroa origanifolia fruits
spellingShingle Antimicrobial activity of an aspartic protease from Salpichroa origanifolia fruits
Díaz, María Eugenia
antimicrobials
cytotoxicity
fungi
proteinase
Staphylococci
title_short Antimicrobial activity of an aspartic protease from Salpichroa origanifolia fruits
title_full Antimicrobial activity of an aspartic protease from Salpichroa origanifolia fruits
title_fullStr Antimicrobial activity of an aspartic protease from Salpichroa origanifolia fruits
title_full_unstemmed Antimicrobial activity of an aspartic protease from Salpichroa origanifolia fruits
title_sort Antimicrobial activity of an aspartic protease from Salpichroa origanifolia fruits
dc.creator.none.fl_str_mv Díaz, María Eugenia
Rocha, Gabriela Fernanda
Kise, Francisco
Rosso, A. M.
Guevara, Maria Gabriela
Parisi, M.G.
author Díaz, María Eugenia
author_facet Díaz, María Eugenia
Rocha, Gabriela Fernanda
Kise, Francisco
Rosso, A. M.
Guevara, Maria Gabriela
Parisi, M.G.
author_role author
author2 Rocha, Gabriela Fernanda
Kise, Francisco
Rosso, A. M.
Guevara, Maria Gabriela
Parisi, M.G.
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv antimicrobials
cytotoxicity
fungi
proteinase
Staphylococci
topic antimicrobials
cytotoxicity
fungi
proteinase
Staphylococci
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Abstract: Plant proteases play a fundamental role in several processes like growth, development and in response to biotic and abiotic stress. In particular, aspartic proteases (AP) are expressed in different plant organs and have antimicrobial activity. Previously, we purified an AP from Salpichroa origanifolia fruits called salpichroin. The aim of this work was to determine the cytotoxic activity of this enzyme on selected plant and human pathogens. For this purpose, the growth of the selected pathogens was analysed after exposure to different concentrations of salpichroin. The results showed that the enzyme was capable of inhibiting Fusarium solani and Staphylococcus aureus in a dose-dependent manner. It was determined that 1·2 μmol l−1 of salpichroin was necessary to inhibit 50% of conidial germination, and the minimal bactericidal concentration was between 1·9 and 2·5 μmol l−1. Using SYTOX Green dye we were able to demonstrate that salpichroin cause membrane permeabilization. Moreover, the enzyme treated with its specific inhibitor pepstatin A did not lose its antibacterial activity. This finding demonstrates that the cytotoxic activity of salpichroin is due to the alteration of the cell plasma membrane barrier but not due to its proteolytic activity. Antimicrobial activity of the AP could represent a potential alternative for the control of pathogens that affect humans or crops of economic interest. Significance and Impact of the Study: This study provides insights into the antimicrobial activity of an aspartic protease isolated from Salpichroa origanifolia fruits on plant and human pathogens. The proteinase inhibited Fusarium solani and Staphylococcus aureus in a dose-dependent manner due to the alteration of the cell plasma membrane barrier but not due to its proteolytic activity. Antimicrobial activity of salpichroin suggests its potential applications as an important tool for the control of pathogenic micro-organisms affecting humans and crops of economic interest. Therefore, it would represent a new alternative to avoid the problems of environmental pollution and antimicrobial resistance.
Fil: Díaz, María Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Luján; Argentina
Fil: Rocha, Gabriela Fernanda. Universidad Nacional de Luján; Argentina
Fil: Kise, Francisco. Universidad Nacional de Luján; Argentina
Fil: Rosso, A. M.. Universidad Nacional de Luján; Argentina
Fil: Guevara, Maria Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: Parisi, M.G.. Universidad Nacional de Luján; Argentina
description Abstract: Plant proteases play a fundamental role in several processes like growth, development and in response to biotic and abiotic stress. In particular, aspartic proteases (AP) are expressed in different plant organs and have antimicrobial activity. Previously, we purified an AP from Salpichroa origanifolia fruits called salpichroin. The aim of this work was to determine the cytotoxic activity of this enzyme on selected plant and human pathogens. For this purpose, the growth of the selected pathogens was analysed after exposure to different concentrations of salpichroin. The results showed that the enzyme was capable of inhibiting Fusarium solani and Staphylococcus aureus in a dose-dependent manner. It was determined that 1·2 μmol l−1 of salpichroin was necessary to inhibit 50% of conidial germination, and the minimal bactericidal concentration was between 1·9 and 2·5 μmol l−1. Using SYTOX Green dye we were able to demonstrate that salpichroin cause membrane permeabilization. Moreover, the enzyme treated with its specific inhibitor pepstatin A did not lose its antibacterial activity. This finding demonstrates that the cytotoxic activity of salpichroin is due to the alteration of the cell plasma membrane barrier but not due to its proteolytic activity. Antimicrobial activity of the AP could represent a potential alternative for the control of pathogens that affect humans or crops of economic interest. Significance and Impact of the Study: This study provides insights into the antimicrobial activity of an aspartic protease isolated from Salpichroa origanifolia fruits on plant and human pathogens. The proteinase inhibited Fusarium solani and Staphylococcus aureus in a dose-dependent manner due to the alteration of the cell plasma membrane barrier but not due to its proteolytic activity. Antimicrobial activity of salpichroin suggests its potential applications as an important tool for the control of pathogenic micro-organisms affecting humans and crops of economic interest. Therefore, it would represent a new alternative to avoid the problems of environmental pollution and antimicrobial resistance.
publishDate 2018
dc.date.none.fl_str_mv 2018-04-24
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/11336/87396
Díaz, María Eugenia; Rocha, Gabriela Fernanda; Kise, Francisco; Rosso, A. M.; Guevara, Maria Gabriela; et al.; Antimicrobial activity of an aspartic protease from Salpichroa origanifolia fruits; Wiley Blackwell Publishing, Inc; Letters in Applied Microbiology; 67; 2; 24-4-2018; 168-174
0266-8254
CONICET Digital
CONICET
url http://hdl.handle.net/11336/87396
identifier_str_mv Díaz, María Eugenia; Rocha, Gabriela Fernanda; Kise, Francisco; Rosso, A. M.; Guevara, Maria Gabriela; et al.; Antimicrobial activity of an aspartic protease from Salpichroa origanifolia fruits; Wiley Blackwell Publishing, Inc; Letters in Applied Microbiology; 67; 2; 24-4-2018; 168-174
0266-8254
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pubmed/29740840
info:eu-repo/semantics/altIdentifier/doi/10.1111/lam.13006
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 Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, 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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