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Characterisation of a flavonoid ligand of the fungal protein Alt a 1
Spores of pathogenic fungi are virtually ubiquitous and cause human disease and severe losses in crops. The endophytic fungi Alternaria species produce host-selective phytotoxins. Alt a 1 is a strongly allergenic protein found in A. alternata that causes severe asthma. Despite the well-established p...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5025882/ https://www.ncbi.nlm.nih.gov/pubmed/27633190 http://dx.doi.org/10.1038/srep33468 |
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author | Garrido-Arandia, María Silva-Navas, Javier Ramírez-Castillejo, Carmen Cubells-Baeza, Nuria Gómez-Casado, Cristina Barber, Domingo Pozo, Juan C. Melendi, Pablo G. Pacios, Luis F. Díaz-Perales, Araceli |
author_facet | Garrido-Arandia, María Silva-Navas, Javier Ramírez-Castillejo, Carmen Cubells-Baeza, Nuria Gómez-Casado, Cristina Barber, Domingo Pozo, Juan C. Melendi, Pablo G. Pacios, Luis F. Díaz-Perales, Araceli |
author_sort | Garrido-Arandia, María |
collection | PubMed |
description | Spores of pathogenic fungi are virtually ubiquitous and cause human disease and severe losses in crops. The endophytic fungi Alternaria species produce host-selective phytotoxins. Alt a 1 is a strongly allergenic protein found in A. alternata that causes severe asthma. Despite the well-established pathogenicity of Alt a 1, the molecular mechanisms underlying its action and physiological function remain largely unknown. To gain insight into the role played by this protein in the pathogenicity of the fungus, we studied production of Alt a 1 and its activity in spores. We found that Alt a 1 accumulates inside spores and that its release with a ligand is pH-dependent, with optimum production in the 5.0–6.5 interval. The Alt a 1 ligand was identified as a methylated flavonoid that inhibits plant root growth and detoxifies reactive oxygen species. We also found that Alt a 1 changes its oligomerization state depending on the pH of the surrounding medium and that these changes facilitate the release of the ligand. Based on these results, we propose that release of Alt a 1 should be a pathogenic target in approaches used to block plant defenses and consequently to favor fungal entry into the plant. |
format | Online Article Text |
id | pubmed-5025882 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-50258822016-09-22 Characterisation of a flavonoid ligand of the fungal protein Alt a 1 Garrido-Arandia, María Silva-Navas, Javier Ramírez-Castillejo, Carmen Cubells-Baeza, Nuria Gómez-Casado, Cristina Barber, Domingo Pozo, Juan C. Melendi, Pablo G. Pacios, Luis F. Díaz-Perales, Araceli Sci Rep Article Spores of pathogenic fungi are virtually ubiquitous and cause human disease and severe losses in crops. The endophytic fungi Alternaria species produce host-selective phytotoxins. Alt a 1 is a strongly allergenic protein found in A. alternata that causes severe asthma. Despite the well-established pathogenicity of Alt a 1, the molecular mechanisms underlying its action and physiological function remain largely unknown. To gain insight into the role played by this protein in the pathogenicity of the fungus, we studied production of Alt a 1 and its activity in spores. We found that Alt a 1 accumulates inside spores and that its release with a ligand is pH-dependent, with optimum production in the 5.0–6.5 interval. The Alt a 1 ligand was identified as a methylated flavonoid that inhibits plant root growth and detoxifies reactive oxygen species. We also found that Alt a 1 changes its oligomerization state depending on the pH of the surrounding medium and that these changes facilitate the release of the ligand. Based on these results, we propose that release of Alt a 1 should be a pathogenic target in approaches used to block plant defenses and consequently to favor fungal entry into the plant. Nature Publishing Group 2016-09-16 /pmc/articles/PMC5025882/ /pubmed/27633190 http://dx.doi.org/10.1038/srep33468 Text en Copyright © 2016, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Garrido-Arandia, María Silva-Navas, Javier Ramírez-Castillejo, Carmen Cubells-Baeza, Nuria Gómez-Casado, Cristina Barber, Domingo Pozo, Juan C. Melendi, Pablo G. Pacios, Luis F. Díaz-Perales, Araceli Characterisation of a flavonoid ligand of the fungal protein Alt a 1 |
title | Characterisation of a flavonoid ligand of the fungal protein Alt a 1 |
title_full | Characterisation of a flavonoid ligand of the fungal protein Alt a 1 |
title_fullStr | Characterisation of a flavonoid ligand of the fungal protein Alt a 1 |
title_full_unstemmed | Characterisation of a flavonoid ligand of the fungal protein Alt a 1 |
title_short | Characterisation of a flavonoid ligand of the fungal protein Alt a 1 |
title_sort | characterisation of a flavonoid ligand of the fungal protein alt a 1 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5025882/ https://www.ncbi.nlm.nih.gov/pubmed/27633190 http://dx.doi.org/10.1038/srep33468 |
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