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Plant immunity suppression by an exo-β-1,3-glucanase and an elongation factor 1α of the rice blast fungus

Fungal cell walls undergo continual remodeling that generates β-1,3-glucan fragments as products of endo-glycosyl hydrolases (GHs), which can be recognized as pathogen-associated molecular patterns (PAMPs) and trigger plant immune responses. How fungal pathogens suppress those responses is often poo...

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Autores principales: Liu, Hang, Lu, Xunli, Li, Mengfei, Lun, Zhiqin, Yan, Xia, Yin, Changfa, Yuan, Guixin, Wang, Xingbin, Liu, Ning, Liu, Di, Wu, Mian, Luo, Ziluolong, Zhang, Yan, Bhadauria, Vijai, Yang, Jun, Talbot, Nicholas J., Peng, You-Liang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10484928/
https://www.ncbi.nlm.nih.gov/pubmed/37679340
http://dx.doi.org/10.1038/s41467-023-41175-z
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author Liu, Hang
Lu, Xunli
Li, Mengfei
Lun, Zhiqin
Yan, Xia
Yin, Changfa
Yuan, Guixin
Wang, Xingbin
Liu, Ning
Liu, Di
Wu, Mian
Luo, Ziluolong
Zhang, Yan
Bhadauria, Vijai
Yang, Jun
Talbot, Nicholas J.
Peng, You-Liang
author_facet Liu, Hang
Lu, Xunli
Li, Mengfei
Lun, Zhiqin
Yan, Xia
Yin, Changfa
Yuan, Guixin
Wang, Xingbin
Liu, Ning
Liu, Di
Wu, Mian
Luo, Ziluolong
Zhang, Yan
Bhadauria, Vijai
Yang, Jun
Talbot, Nicholas J.
Peng, You-Liang
author_sort Liu, Hang
collection PubMed
description Fungal cell walls undergo continual remodeling that generates β-1,3-glucan fragments as products of endo-glycosyl hydrolases (GHs), which can be recognized as pathogen-associated molecular patterns (PAMPs) and trigger plant immune responses. How fungal pathogens suppress those responses is often poorly understood. Here, we study mechanisms underlying the suppression of β-1,3-glucan-triggered plant immunity by the blast fungus Magnaporthe oryzae. We show that an exo-β-1,3-glucanase of the GH17 family, named Ebg1, is important for fungal cell wall integrity and virulence of M. oryzae. Ebg1 can hydrolyze β-1,3-glucan and laminarin into glucose, thus suppressing β-1,3-glucan-triggered plant immunity. However, in addition, Ebg1 seems to act as a PAMP, independent of its hydrolase activity. This Ebg1-induced immunity appears to be dampened by the secretion of an elongation factor 1 alpha protein (EF1α), which interacts and co-localizes with Ebg1 in the apoplast. Future work is needed to understand the mechanisms behind Ebg1-induced immunity and its suppression by EF1α.
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spelling pubmed-104849282023-09-09 Plant immunity suppression by an exo-β-1,3-glucanase and an elongation factor 1α of the rice blast fungus Liu, Hang Lu, Xunli Li, Mengfei Lun, Zhiqin Yan, Xia Yin, Changfa Yuan, Guixin Wang, Xingbin Liu, Ning Liu, Di Wu, Mian Luo, Ziluolong Zhang, Yan Bhadauria, Vijai Yang, Jun Talbot, Nicholas J. Peng, You-Liang Nat Commun Article Fungal cell walls undergo continual remodeling that generates β-1,3-glucan fragments as products of endo-glycosyl hydrolases (GHs), which can be recognized as pathogen-associated molecular patterns (PAMPs) and trigger plant immune responses. How fungal pathogens suppress those responses is often poorly understood. Here, we study mechanisms underlying the suppression of β-1,3-glucan-triggered plant immunity by the blast fungus Magnaporthe oryzae. We show that an exo-β-1,3-glucanase of the GH17 family, named Ebg1, is important for fungal cell wall integrity and virulence of M. oryzae. Ebg1 can hydrolyze β-1,3-glucan and laminarin into glucose, thus suppressing β-1,3-glucan-triggered plant immunity. However, in addition, Ebg1 seems to act as a PAMP, independent of its hydrolase activity. This Ebg1-induced immunity appears to be dampened by the secretion of an elongation factor 1 alpha protein (EF1α), which interacts and co-localizes with Ebg1 in the apoplast. Future work is needed to understand the mechanisms behind Ebg1-induced immunity and its suppression by EF1α. Nature Publishing Group UK 2023-09-07 /pmc/articles/PMC10484928/ /pubmed/37679340 http://dx.doi.org/10.1038/s41467-023-41175-z Text en © The Author(s) 2023 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
Liu, Hang
Lu, Xunli
Li, Mengfei
Lun, Zhiqin
Yan, Xia
Yin, Changfa
Yuan, Guixin
Wang, Xingbin
Liu, Ning
Liu, Di
Wu, Mian
Luo, Ziluolong
Zhang, Yan
Bhadauria, Vijai
Yang, Jun
Talbot, Nicholas J.
Peng, You-Liang
Plant immunity suppression by an exo-β-1,3-glucanase and an elongation factor 1α of the rice blast fungus
title Plant immunity suppression by an exo-β-1,3-glucanase and an elongation factor 1α of the rice blast fungus
title_full Plant immunity suppression by an exo-β-1,3-glucanase and an elongation factor 1α of the rice blast fungus
title_fullStr Plant immunity suppression by an exo-β-1,3-glucanase and an elongation factor 1α of the rice blast fungus
title_full_unstemmed Plant immunity suppression by an exo-β-1,3-glucanase and an elongation factor 1α of the rice blast fungus
title_short Plant immunity suppression by an exo-β-1,3-glucanase and an elongation factor 1α of the rice blast fungus
title_sort plant immunity suppression by an exo-β-1,3-glucanase and an elongation factor 1α of the rice blast fungus
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10484928/
https://www.ncbi.nlm.nih.gov/pubmed/37679340
http://dx.doi.org/10.1038/s41467-023-41175-z
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