The Antifungal Peptide MCh-AMP1 Derived From Matricaria chamomilla Inhibits Candida albicans Growth via Inducing ROS Generation and Altering Fungal Cell Membrane Permeability
The rise of antifungal drug resistance in Candida species responsible for life threatening candidiasis is considered as an increasing challenge for the public health. MCh-AMP1 has previously been reported as a natural peptide from Matricaria chamomilla L. flowers with broad-spectrum antifungal activ...
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Frontiers Media S.A.
2020-01-01
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Online Access: | https://www.frontiersin.org/article/10.3389/fmicb.2019.03150/full |
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author | Sima Sadat Seyedjavadi Soghra Khani Ali Eslamifar Soheila Ajdary Mehdi Goudarzi Raheleh Halabian Reza Akbari Hadi Zare-Zardini Abbas Ali Imani Fooladi Jafar Amani Mehdi Razzaghi-Abyaneh |
author_facet | Sima Sadat Seyedjavadi Soghra Khani Ali Eslamifar Soheila Ajdary Mehdi Goudarzi Raheleh Halabian Reza Akbari Hadi Zare-Zardini Abbas Ali Imani Fooladi Jafar Amani Mehdi Razzaghi-Abyaneh |
author_sort | Sima Sadat Seyedjavadi |
collection | DOAJ |
description | The rise of antifungal drug resistance in Candida species responsible for life threatening candidiasis is considered as an increasing challenge for the public health. MCh-AMP1 has previously been reported as a natural peptide from Matricaria chamomilla L. flowers with broad-spectrum antifungal activity against human pathogenic molds and yeasts. In the current study, the mode of action of synthetic MCh-AMP1 was investigated against Candida albicans, the major etiologic agent of life-threatening nosocomial candidiasis at cellular and molecular levels. Candida albicans ATCC 10231 was cultured in presence of various concentrations of MCh-AMP1 (16–64 μg/mL) and its mode of action was investigated using plasma membrane permeabilization assays, reactive oxygen species (ROS) induction, potassium ion leakage and ultrastructural analyses by electron microscopy. MCh-AMP1 showed fungicidal activity against Candida albicans at the concentrations of 32 and 64 μg/mL. The peptide increased fungal cell membrane permeability as evidenced by elevating of PI uptake and induced potassium leakage from the yeast cells. ROS production was induced by the peptide inside the fungal cells to a maximum of 64.8% at the concentration of 64 μg/mL. Scanning electron microscopy observations showed cell deformation as shrinkage and folding of treated yeast cells. Transmission electron microscopy showed detachment of plasma membrane from the cell wall, cell depletion and massive destruction of intracellular organelles and cell membrane of the fungal cells. Our results demonstrated that MCh-AMP1 caused Candida albicans cell death via increasing cell membrane permeability and inducing ROS production. Therefore, MCh-AMP1 could be considered as a promising therapeutic agent to combat Candida albicans infections. |
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issn | 1664-302X |
language | English |
last_indexed | 2024-12-12T23:33:40Z |
publishDate | 2020-01-01 |
publisher | Frontiers Media S.A. |
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spelling | doaj.art-8ce87fbd207e416b9d9aac5851ff535f2022-12-22T00:07:38ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2020-01-011010.3389/fmicb.2019.03150474453The Antifungal Peptide MCh-AMP1 Derived From Matricaria chamomilla Inhibits Candida albicans Growth via Inducing ROS Generation and Altering Fungal Cell Membrane PermeabilitySima Sadat Seyedjavadi0Soghra Khani1Ali Eslamifar2Soheila Ajdary3Mehdi Goudarzi4Raheleh Halabian5Reza Akbari6Hadi Zare-Zardini7Abbas Ali Imani Fooladi8Jafar Amani9Mehdi Razzaghi-Abyaneh10Department of Mycology, Pasteur Institute of Iran, Tehran, IranDepartment of Mycology, Pasteur Institute of Iran, Tehran, IranDepartment of Clinical Research, Pasteur Institute of Iran, Tehran, IranDepartment of Immunology, Pasteur Institute of Iran, Tehran, IranDepartment of Microbiology, School of Medicine, Shahid Beheshti University of Medical Sciences, Tehran, IranApplied Microbiology Research Center, Systems Biology and Poisonings Institute, Baqiyatallah University of Medical Sciences, Tehran, IranDepartment of Microbiology, Faculty of Medicine, Urmia University of Medical Sciences, Urmia, IranHematology and Oncology Research Center, Shahid Sadoughi University of Medical Sciences, Yazd, IranApplied Microbiology Research Center, Systems Biology and Poisonings Institute, Baqiyatallah University of Medical Sciences, Tehran, IranApplied Microbiology Research Center, Systems Biology and Poisonings Institute, Baqiyatallah University of Medical Sciences, Tehran, IranDepartment of Mycology, Pasteur Institute of Iran, Tehran, IranThe rise of antifungal drug resistance in Candida species responsible for life threatening candidiasis is considered as an increasing challenge for the public health. MCh-AMP1 has previously been reported as a natural peptide from Matricaria chamomilla L. flowers with broad-spectrum antifungal activity against human pathogenic molds and yeasts. In the current study, the mode of action of synthetic MCh-AMP1 was investigated against Candida albicans, the major etiologic agent of life-threatening nosocomial candidiasis at cellular and molecular levels. Candida albicans ATCC 10231 was cultured in presence of various concentrations of MCh-AMP1 (16–64 μg/mL) and its mode of action was investigated using plasma membrane permeabilization assays, reactive oxygen species (ROS) induction, potassium ion leakage and ultrastructural analyses by electron microscopy. MCh-AMP1 showed fungicidal activity against Candida albicans at the concentrations of 32 and 64 μg/mL. The peptide increased fungal cell membrane permeability as evidenced by elevating of PI uptake and induced potassium leakage from the yeast cells. ROS production was induced by the peptide inside the fungal cells to a maximum of 64.8% at the concentration of 64 μg/mL. Scanning electron microscopy observations showed cell deformation as shrinkage and folding of treated yeast cells. Transmission electron microscopy showed detachment of plasma membrane from the cell wall, cell depletion and massive destruction of intracellular organelles and cell membrane of the fungal cells. Our results demonstrated that MCh-AMP1 caused Candida albicans cell death via increasing cell membrane permeability and inducing ROS production. Therefore, MCh-AMP1 could be considered as a promising therapeutic agent to combat Candida albicans infections.https://www.frontiersin.org/article/10.3389/fmicb.2019.03150/fullantifungal peptidespeptide synthesisCandida albicansantifungal activitytime killing assayelectron microscopy |
spellingShingle | Sima Sadat Seyedjavadi Soghra Khani Ali Eslamifar Soheila Ajdary Mehdi Goudarzi Raheleh Halabian Reza Akbari Hadi Zare-Zardini Abbas Ali Imani Fooladi Jafar Amani Mehdi Razzaghi-Abyaneh The Antifungal Peptide MCh-AMP1 Derived From Matricaria chamomilla Inhibits Candida albicans Growth via Inducing ROS Generation and Altering Fungal Cell Membrane Permeability Frontiers in Microbiology antifungal peptides peptide synthesis Candida albicans antifungal activity time killing assay electron microscopy |
title | The Antifungal Peptide MCh-AMP1 Derived From Matricaria chamomilla Inhibits Candida albicans Growth via Inducing ROS Generation and Altering Fungal Cell Membrane Permeability |
title_full | The Antifungal Peptide MCh-AMP1 Derived From Matricaria chamomilla Inhibits Candida albicans Growth via Inducing ROS Generation and Altering Fungal Cell Membrane Permeability |
title_fullStr | The Antifungal Peptide MCh-AMP1 Derived From Matricaria chamomilla Inhibits Candida albicans Growth via Inducing ROS Generation and Altering Fungal Cell Membrane Permeability |
title_full_unstemmed | The Antifungal Peptide MCh-AMP1 Derived From Matricaria chamomilla Inhibits Candida albicans Growth via Inducing ROS Generation and Altering Fungal Cell Membrane Permeability |
title_short | The Antifungal Peptide MCh-AMP1 Derived From Matricaria chamomilla Inhibits Candida albicans Growth via Inducing ROS Generation and Altering Fungal Cell Membrane Permeability |
title_sort | antifungal peptide mch amp1 derived from matricaria chamomilla inhibits candida albicans growth via inducing ros generation and altering fungal cell membrane permeability |
topic | antifungal peptides peptide synthesis Candida albicans antifungal activity time killing assay electron microscopy |
url | https://www.frontiersin.org/article/10.3389/fmicb.2019.03150/full |
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