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作 者:Ning Liu Linlu Qi Manna Huang Deng Chen Changfa Yin Yiying Zhang Xingbin Wang Guixin Yuan Rui-Jin Wang Jun Yang You-Liang Peng Xunli Lu
机构地区:[1]State Key Laboratory of Agrobiotechnology and MOA Key Laboratory of Pest Monitoring and Green Management,China Agricultural University,Beijing 100193,China [2]MOA Key Laboratory of Pest Monitoring and Green Management,College of Plant Protection,China Agricultural University,Beijing 100193,China [3]Graduate School of China Agricultural University,Beijing 100193,China
出 处:《Genomics, Proteomics & Bioinformatics》2022年第4期728-746,共19页基因组蛋白质组与生物信息学报(英文版)
基 金:supported by the National Key R&D Plan of China(Grant No.2016YFD0300703);the China Agricultural Research System(Grant No.CARS-01-33);the Program for Changjiang Scholars and Innovative Research Team in University(Grant No.IRT1042);the 111 Project(Grant No.B13006)to YLP;the National Natural Science Foundation of China(Grant No.32001848)to XL。
摘 要:Plant fungal pathogens secrete numerous proteins into the apoplast at the plant–fungus contact sites to facilitate colonization.However,only a few secretory proteins were functionally characterized in Magnaporthe oryzae,the fungal pathogen causing rice blast disease worldwide.Asparagine-linked glycosylation 3(Alg3)is an a-1,3-mannosyltransferase functioning in the Nglycan synthesis of N-glycosylated secretory proteins.Fungal pathogenicity and cell wall integrity are impaired inΔalg3 mutants,but the secreted proteins affected inΔalg3 mutants are largely unknown.In this study,we compared the secretomes of the wild-type strain and theΔalg3 mutant and identified 51 proteins that require Alg3 for proper secretion.These proteins were predicted to be involved in metabolic processes,interspecies interactions,cell wall organization,and response to chemicals.Nine proteins were selected for further validation.We found that these proteins were localized at the apoplastic region surrounding the fungal infection hyphae.Moreover,the Nglycosylation of these proteins was significantly changed in theΔalg3 mutant,leading to the decreased protein secretion and abnormal protein localization.Furthermore,we tested the biological functions of two genes,INV1(encoding invertase 1,a secreted invertase)and AMCase(encoding acid mammalian chinitase,a secreted chitinase).The fungal virulence was significantly reduced,and the cell wall integrity was altered in theΔinv1 andΔamcase mutant strains.Moreover,the N-glycosylation was essential for the function and secretion of AMCase.Taken together,our study provides new insight into the role of N-glycosylated secretory proteins in fungal virulence and cell wall integrity.
关 键 词:Magnaporthe oryzae SECRETOME N-GLYCOSYLATION Invertase 1 Acid mammalian chinitase
分 类 号:S435.111.41[农业科学—农业昆虫与害虫防治]
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