Antimicrobial activity of an aspartic protease from Salpichroa origanifolia fruits
| Autor: | Francisco Kise, Mónica G. Parisi, Gabriela F. Rocha, María Gabriela Guevara, María Eugenia Díaz, Adriana Mabel Rosso |
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| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Fusarium Staphylococcus aureus Antifungal Agents Aspartic Acid Proteases 030106 microbiology Microbial Sensitivity Tests medicine.disease_cause Applied Microbiology and Biotechnology Permeability antimicrobials Microbiology Ciencias Biológicas purl.org/becyt/ford/1 [https] 03 medical and health sciences Biología Celular Microbiología Aspartate protease medicine Humans Cytotoxicity purl.org/becyt/ford/1.6 [https] Solanaceae Salpichroa origanifolia Staphylococci biology Chemistry Cell Membrane biology.organism_classification Antimicrobial Anti-Bacterial Agents Fruit cytotoxicity proteinase fungi CIENCIAS NATURALES Y EXACTAS |
| Zdroj: | CONICET Digital (CONICET) Consejo Nacional de Investigaciones Científicas y Técnicas instacron:CONICET |
| Popis: | 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 |
| Databáze: | OpenAIRE |
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