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Antifungal activity of an artificial peptide aptamer SNP-D4 against Fusarium oxysporum
Fusarium oxysporum f. sp. cubense (FOC4) is a pathogen of banana fusarium wilt, which is a serious problem that has plagued the tropical banana industry for many years. The pathogenic mechanism is complex and unclear, so the prevention and control in agricultural production applications is ineffecti...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
PeerJ Inc.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8877334/ https://www.ncbi.nlm.nih.gov/pubmed/35223198 http://dx.doi.org/10.7717/peerj.12756 |
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author | Huang, Junjun Wang, Dan Li, Hong Tang, Yanqiong Ma, Xiang Tang, Hongqian Lin, Min Liu, Zhu |
author_facet | Huang, Junjun Wang, Dan Li, Hong Tang, Yanqiong Ma, Xiang Tang, Hongqian Lin, Min Liu, Zhu |
author_sort | Huang, Junjun |
collection | PubMed |
description | Fusarium oxysporum f. sp. cubense (FOC4) is a pathogen of banana fusarium wilt, which is a serious problem that has plagued the tropical banana industry for many years. The pathogenic mechanism is complex and unclear, so the prevention and control in agricultural production applications is ineffective. SNP-D4, an artificial peptide aptamer, was identified and specifically inhibited FOC4. To evaluate the efficacy of SNP-D4, FoC4 spores were treated with purified SNP-D4 to calculate the germination and fungicide rates. Damage of FOC4 spores was observed by staining with propidium iodide (PI). Eight proteins of FOC4 were identified to have high affinity for SNP-D4 by a pull-down method combined with Q-Exactive mass spectrometry. Of these eight proteins, A0A5C6SPC6, the aldehyde dehydrogenase of FOC4, was selected as an example to scrutinize the interaction sites with SNP-D4. Molecular docking revealed that Thr66 on the peptide loop of SNP-D4 bound with Tyr437 near the catalytic center of A0A5C6SPC6. Subsequently 42 spore proteins which exhibited associations with the eight proteins were retrieved for protein-protein interaction analysis, demonstrating that SNP-D4 interfered with pathways including ‘translation’, ‘folding, sorting and degradation’, ‘transcription’, ‘signal transduction’ and ‘cell growth and death’, eventually causing the inhibition of growth of FOC4. This study not only investigated the possible pathogenic mechanism of FOC4, but also provided a potential antifungal agent SNP-D4 for use in the control of banana wilt disease. |
format | Online Article Text |
id | pubmed-8877334 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | PeerJ Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-88773342022-02-26 Antifungal activity of an artificial peptide aptamer SNP-D4 against Fusarium oxysporum Huang, Junjun Wang, Dan Li, Hong Tang, Yanqiong Ma, Xiang Tang, Hongqian Lin, Min Liu, Zhu PeerJ Agricultural Science Fusarium oxysporum f. sp. cubense (FOC4) is a pathogen of banana fusarium wilt, which is a serious problem that has plagued the tropical banana industry for many years. The pathogenic mechanism is complex and unclear, so the prevention and control in agricultural production applications is ineffective. SNP-D4, an artificial peptide aptamer, was identified and specifically inhibited FOC4. To evaluate the efficacy of SNP-D4, FoC4 spores were treated with purified SNP-D4 to calculate the germination and fungicide rates. Damage of FOC4 spores was observed by staining with propidium iodide (PI). Eight proteins of FOC4 were identified to have high affinity for SNP-D4 by a pull-down method combined with Q-Exactive mass spectrometry. Of these eight proteins, A0A5C6SPC6, the aldehyde dehydrogenase of FOC4, was selected as an example to scrutinize the interaction sites with SNP-D4. Molecular docking revealed that Thr66 on the peptide loop of SNP-D4 bound with Tyr437 near the catalytic center of A0A5C6SPC6. Subsequently 42 spore proteins which exhibited associations with the eight proteins were retrieved for protein-protein interaction analysis, demonstrating that SNP-D4 interfered with pathways including ‘translation’, ‘folding, sorting and degradation’, ‘transcription’, ‘signal transduction’ and ‘cell growth and death’, eventually causing the inhibition of growth of FOC4. This study not only investigated the possible pathogenic mechanism of FOC4, but also provided a potential antifungal agent SNP-D4 for use in the control of banana wilt disease. PeerJ Inc. 2022-02-22 /pmc/articles/PMC8877334/ /pubmed/35223198 http://dx.doi.org/10.7717/peerj.12756 Text en © 2022 Huang et al. https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ) and either DOI or URL of the article must be cited. |
spellingShingle | Agricultural Science Huang, Junjun Wang, Dan Li, Hong Tang, Yanqiong Ma, Xiang Tang, Hongqian Lin, Min Liu, Zhu Antifungal activity of an artificial peptide aptamer SNP-D4 against Fusarium oxysporum |
title | Antifungal activity of an artificial peptide aptamer SNP-D4 against Fusarium oxysporum |
title_full | Antifungal activity of an artificial peptide aptamer SNP-D4 against Fusarium oxysporum |
title_fullStr | Antifungal activity of an artificial peptide aptamer SNP-D4 against Fusarium oxysporum |
title_full_unstemmed | Antifungal activity of an artificial peptide aptamer SNP-D4 against Fusarium oxysporum |
title_short | Antifungal activity of an artificial peptide aptamer SNP-D4 against Fusarium oxysporum |
title_sort | antifungal activity of an artificial peptide aptamer snp-d4 against fusarium oxysporum |
topic | Agricultural Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8877334/ https://www.ncbi.nlm.nih.gov/pubmed/35223198 http://dx.doi.org/10.7717/peerj.12756 |
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