TY - JOUR
T1 - Plant immunity suppression by an exo-β-1,3-glucanase and an elongation factor 1α of the rice blast fungus
AU - Liu, Hang
AU - Lu, Xunli
AU - Li, Mengfei
AU - Lun, Zhiqin
AU - Yan, Xia
AU - Yin, Changfa
AU - Yuan, Guixin
AU - Wang, Xingbin
AU - Liu, Ning
AU - Liu, Di
AU - Wu, Mian
AU - Luo, Ziluolong
AU - Zhang, Yan
AU - Bhadauria, Vijai
AU - Yang, Jun
AU - Talbot, Nicholas J.
AU - Peng, You Liang
N1 - Data availability statement: The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the iProX partner repository with the dataset identifier PXD024706 and PXD044578. Source data are provided with this paper.
Funding Information: This work was supported by the National Key Research and Development Program from Ministry of Science and Technology, China [grant 2016YFD0300703] to Y.-L.P., the National Natural Science Foundation of China [Grant No. 32172370] to X.L., the China Agricultural Research System from Ministry of Agriculture and Rural Affairs [CARS-01-43], the CSIRT Program [IRT1042] and the 111 Project [B13006] from Ministry of Education, China, and the Pinduoduo-China Agricultural University Research Fund to Y.-L.P. N.J.T. is funded by the Gatsby Charitable Foundation, the Biotechnology and Biological Sciences Research Council (BBS/E/J/000PR9797) and is a partner in 111 Project [B13006]. The funders had no role in study design, data collection and analysis, the decision to publish, or preparation of the manuscript.
PY - 2023/9/7
Y1 - 2023/9/7
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85170184145&partnerID=8YFLogxK
U2 - 10.1038/s41467-023-41175-z
DO - 10.1038/s41467-023-41175-z
M3 - Article
C2 - 37679340
AN - SCOPUS:85170184145
SN - 2041-1723
VL - 14
JO - Nature Communications
JF - Nature Communications
M1 - 5491
ER -