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Antifungal activity of MAF-1A peptide against Candida albicans
Invasive candidiasis is a major threat to human health, and Candida albicans is the most common pathogenic species responsible for this condition. The incidence of drug-resistant strains of C. albicans is rising, necessitating the development of new antifungal drugs. Antimicrobial peptides (AMPs) ha...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer International Publishing
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8046747/ https://www.ncbi.nlm.nih.gov/pubmed/33452940 http://dx.doi.org/10.1007/s10123-021-00159-z |
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author | Cheng, Rong Xu, Qiang Hu, Fangfang Li, Hongling Yang, Bin Duan, Zonggang Zhang, Kai Wu, Jianwei Li, Wei Luo, Zhenhua |
author_facet | Cheng, Rong Xu, Qiang Hu, Fangfang Li, Hongling Yang, Bin Duan, Zonggang Zhang, Kai Wu, Jianwei Li, Wei Luo, Zhenhua |
author_sort | Cheng, Rong |
collection | PubMed |
description | Invasive candidiasis is a major threat to human health, and Candida albicans is the most common pathogenic species responsible for this condition. The incidence of drug-resistant strains of C. albicans is rising, necessitating the development of new antifungal drugs. Antimicrobial peptides (AMPs) have recently attracted attention due to their unique ability to evade the drug resistance of microorganisms. However, the mechanism of their activity has not yet been identified. The current study analyzed the mode of action of MAF-1A by confocal microscopy, scanning electron microscopy, fluorescent staining, flow cytometry, and qRT-PCR. The results indicate that MAF-1A disrupts the cell membrane of C. albicans and enters the cell where it binds and interacts with nucleic acids. qRT-PCR demonstrated that the expression of several sterol biosynthesis–related genes in C. albicans was increased after MAF-1A treatment. Together, these findings suggest that MAF-1A exerts antifungal action by affecting both the cell membrane and intracellular components. The antifungal mechanism of MAF-1A is unique, and its identification has great research and clinical significance. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s10123-021-00159-z. |
format | Online Article Text |
id | pubmed-8046747 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Springer International Publishing |
record_format | MEDLINE/PubMed |
spelling | pubmed-80467472021-04-29 Antifungal activity of MAF-1A peptide against Candida albicans Cheng, Rong Xu, Qiang Hu, Fangfang Li, Hongling Yang, Bin Duan, Zonggang Zhang, Kai Wu, Jianwei Li, Wei Luo, Zhenhua Int Microbiol Original Article Invasive candidiasis is a major threat to human health, and Candida albicans is the most common pathogenic species responsible for this condition. The incidence of drug-resistant strains of C. albicans is rising, necessitating the development of new antifungal drugs. Antimicrobial peptides (AMPs) have recently attracted attention due to their unique ability to evade the drug resistance of microorganisms. However, the mechanism of their activity has not yet been identified. The current study analyzed the mode of action of MAF-1A by confocal microscopy, scanning electron microscopy, fluorescent staining, flow cytometry, and qRT-PCR. The results indicate that MAF-1A disrupts the cell membrane of C. albicans and enters the cell where it binds and interacts with nucleic acids. qRT-PCR demonstrated that the expression of several sterol biosynthesis–related genes in C. albicans was increased after MAF-1A treatment. Together, these findings suggest that MAF-1A exerts antifungal action by affecting both the cell membrane and intracellular components. The antifungal mechanism of MAF-1A is unique, and its identification has great research and clinical significance. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s10123-021-00159-z. Springer International Publishing 2021-01-16 2021 /pmc/articles/PMC8046747/ /pubmed/33452940 http://dx.doi.org/10.1007/s10123-021-00159-z Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Original Article Cheng, Rong Xu, Qiang Hu, Fangfang Li, Hongling Yang, Bin Duan, Zonggang Zhang, Kai Wu, Jianwei Li, Wei Luo, Zhenhua Antifungal activity of MAF-1A peptide against Candida albicans |
title | Antifungal activity of MAF-1A peptide against Candida albicans |
title_full | Antifungal activity of MAF-1A peptide against Candida albicans |
title_fullStr | Antifungal activity of MAF-1A peptide against Candida albicans |
title_full_unstemmed | Antifungal activity of MAF-1A peptide against Candida albicans |
title_short | Antifungal activity of MAF-1A peptide against Candida albicans |
title_sort | antifungal activity of maf-1a peptide against candida albicans |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8046747/ https://www.ncbi.nlm.nih.gov/pubmed/33452940 http://dx.doi.org/10.1007/s10123-021-00159-z |
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