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The Botrytis cinerea Crh1 transglycosylase is a cytoplasmic effector triggering plant cell death and defense response
Crh proteins catalyze crosslinking of chitin and glucan polymers in fungal cell walls. Here, we show that the BcCrh1 protein from the phytopathogenic fungus Botrytis cinerea acts as a cytoplasmic effector and elicitor of plant defense. BcCrh1 is localized in vacuoles and the endoplasmic reticulum du...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8042016/ https://www.ncbi.nlm.nih.gov/pubmed/33846308 http://dx.doi.org/10.1038/s41467-021-22436-1 |
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author | Bi, Kai Scalschi, Loredana Jaiswal, Namrata Mengiste, Tesfaye Fried, Renana Sanz, Ana Belén Arroyo, Javier Zhu, Wenjun Masrati, Gal Sharon, Amir |
author_facet | Bi, Kai Scalschi, Loredana Jaiswal, Namrata Mengiste, Tesfaye Fried, Renana Sanz, Ana Belén Arroyo, Javier Zhu, Wenjun Masrati, Gal Sharon, Amir |
author_sort | Bi, Kai |
collection | PubMed |
description | Crh proteins catalyze crosslinking of chitin and glucan polymers in fungal cell walls. Here, we show that the BcCrh1 protein from the phytopathogenic fungus Botrytis cinerea acts as a cytoplasmic effector and elicitor of plant defense. BcCrh1 is localized in vacuoles and the endoplasmic reticulum during saprophytic growth. However, upon plant infection, the protein accumulates in infection cushions; it is then secreted to the apoplast and translocated into plant cells, where it induces cell death and defense responses. Two regions of 53 and 35 amino acids are sufficient for protein uptake and cell death induction, respectively. BcCrh1 mutant variants that are unable to dimerize lack transglycosylation activity, but are still able to induce plant cell death. Furthermore, Arabidopsis lines expressing the bccrh1 gene exhibit reduced sensitivity to B. cinerea, suggesting a potential use of the BcCrh1 protein in plant immunization against this necrotrophic pathogen. |
format | Online Article Text |
id | pubmed-8042016 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-80420162021-04-30 The Botrytis cinerea Crh1 transglycosylase is a cytoplasmic effector triggering plant cell death and defense response Bi, Kai Scalschi, Loredana Jaiswal, Namrata Mengiste, Tesfaye Fried, Renana Sanz, Ana Belén Arroyo, Javier Zhu, Wenjun Masrati, Gal Sharon, Amir Nat Commun Article Crh proteins catalyze crosslinking of chitin and glucan polymers in fungal cell walls. Here, we show that the BcCrh1 protein from the phytopathogenic fungus Botrytis cinerea acts as a cytoplasmic effector and elicitor of plant defense. BcCrh1 is localized in vacuoles and the endoplasmic reticulum during saprophytic growth. However, upon plant infection, the protein accumulates in infection cushions; it is then secreted to the apoplast and translocated into plant cells, where it induces cell death and defense responses. Two regions of 53 and 35 amino acids are sufficient for protein uptake and cell death induction, respectively. BcCrh1 mutant variants that are unable to dimerize lack transglycosylation activity, but are still able to induce plant cell death. Furthermore, Arabidopsis lines expressing the bccrh1 gene exhibit reduced sensitivity to B. cinerea, suggesting a potential use of the BcCrh1 protein in plant immunization against this necrotrophic pathogen. Nature Publishing Group UK 2021-04-12 /pmc/articles/PMC8042016/ /pubmed/33846308 http://dx.doi.org/10.1038/s41467-021-22436-1 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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Bi, Kai Scalschi, Loredana Jaiswal, Namrata Mengiste, Tesfaye Fried, Renana Sanz, Ana Belén Arroyo, Javier Zhu, Wenjun Masrati, Gal Sharon, Amir The Botrytis cinerea Crh1 transglycosylase is a cytoplasmic effector triggering plant cell death and defense response |
title | The Botrytis cinerea Crh1 transglycosylase is a cytoplasmic effector triggering plant cell death and defense response |
title_full | The Botrytis cinerea Crh1 transglycosylase is a cytoplasmic effector triggering plant cell death and defense response |
title_fullStr | The Botrytis cinerea Crh1 transglycosylase is a cytoplasmic effector triggering plant cell death and defense response |
title_full_unstemmed | The Botrytis cinerea Crh1 transglycosylase is a cytoplasmic effector triggering plant cell death and defense response |
title_short | The Botrytis cinerea Crh1 transglycosylase is a cytoplasmic effector triggering plant cell death and defense response |
title_sort | botrytis cinerea crh1 transglycosylase is a cytoplasmic effector triggering plant cell death and defense response |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8042016/ https://www.ncbi.nlm.nih.gov/pubmed/33846308 http://dx.doi.org/10.1038/s41467-021-22436-1 |
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