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学者姓名：李元宝
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Abstract ：
Rice blast disease caused by Magnaporthe oryzae poses a severe threat to rice production. To counteract M. oryzae, plants synthesize jasmonate (JA) and lignin, two primary defense-related metabolites, to initiate defense programs. However, the mechanism through which M. oryzae modulates JA- and lignin-mediated plant immunity remains unclear. In this study, a novel M. oryzae effector, MoBys1, was identified as being involved in pathogenesis. Knockout of MoBys1 in M. oryzae significantly reduced its infection ability. Conversely, overexpression of MoBys1 in rice impaired the rice defense response. MoBys1 localizes to the plant cytoplasm and nucleus and interacts with rice cinnamyl alcohol dehydrogenase 2 (OsCAD2), an enzyme that catalyzes lignin biosynthesis. While OsCAD2 mutants exhibited weakened defenses, overexpression lines demonstrated enhanced resistance, highlighting the critical role of OsCAD2 in blast resistance. Furthermore, OsCAD2 functions as a transcription factor regulating a wide range of biological processes, including JA and lignin signaling pathways. The interaction between MoBys1 and OsCAD2 promotes OsCAD2 degradation, leading to reduced lignin and JA accumulation. These findings uncover a novel counter-defense mechanism by which M. oryzae employs the effector MoBys1 to degrade OsCAD2 and suppress host defense-related metabolite accumulation during infection.
Keyword ：
effector effector jasmonate acid jasmonate acid lignin lignin plant defense response plant defense response rice blast rice blast
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| GB/T 7714 | Liu, Chengyu , Han, Li-Bo , Wen, Yanhong et al. The Magnaporthe oryzae effector MoBys1 suppresses rice immunity by targeting OsCAD2 to manipulate host jasmonate and lignin metabolism [J]. | NEW PHYTOLOGIST , 2025 , 246 (1) : 280-297 . |
| MLA | Liu, Chengyu et al. "The Magnaporthe oryzae effector MoBys1 suppresses rice immunity by targeting OsCAD2 to manipulate host jasmonate and lignin metabolism" . | NEW PHYTOLOGIST 246 . 1 (2025) : 280-297 . |
| APA | Liu, Chengyu , Han, Li-Bo , Wen, Yanhong , Lu, Chuner , Deng, Boqian , Liu, Zixuan et al. The Magnaporthe oryzae effector MoBys1 suppresses rice immunity by targeting OsCAD2 to manipulate host jasmonate and lignin metabolism . | NEW PHYTOLOGIST , 2025 , 246 (1) , 280-297 . |
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本文概述了金川雪梨的栽培环境、性状、香气及营养成分，探讨了其加工工艺优化，包括采摘保鲜、加工分级、包装物流等方面。同时，强调了质量控制的重要性，构建了全面品质评价体系，深入分析了营养成分与功能，强化了病虫害防治与农药残留控制，并注重产地环境与可持续发展研究。这些措施旨在提升金川雪梨加工产品的核心竞争力，推动产业绿色发展。
Keyword ：
产地环境 产地环境 加工工艺 加工工艺 绿色发展 绿色发展 质量控制 质量控制 金川雪梨 金川雪梨
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| GB/T 7714 | 冯珂萱 , 骆贤亮 , 李元宝 . 金川雪梨的采摘、加工、物流技术及质量控制措施 [J]. | 中国食品工业 , 2025 , 3 (07) : 110-112 . |
| MLA | 冯珂萱 et al. "金川雪梨的采摘、加工、物流技术及质量控制措施" . | 中国食品工业 3 . 07 (2025) : 110-112 . |
| APA | 冯珂萱 , 骆贤亮 , 李元宝 . 金川雪梨的采摘、加工、物流技术及质量控制措施 . | 中国食品工业 , 2025 , 3 (07) , 110-112 . |
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The polarized actin cable from the Spitzenk & ouml;rper at the hyphal tip fuels filamentous growth in diverse biphasic fungal pathogens. This multicomponent complex, featuring the actin nucleator Bni1 and its associated actin regulator, initiates actin polymerization, guiding biphasic fungal growth and host infection. How dynamic assembly of the Spitzenk & ouml;rper and actin cable is achieved to support filamentous fungi that undergo multistage morphogenesis for host invasion remains unclear. These fungi include Magnaporthe oryzae (M. oryzae), which undergoes a multistage morphological transition during host plant infection. Here, we showed that the M. oryzae scaffolder protein MoSpa2 remodels actin cable networks in space and time by assembling the polarisome complex via phase separation, thereby supporting polarized growth in M. oryzae. Via its N-terminal intrinsically disordered regions, MoSpa2 first stimulates actin cable assembly through multivalent interactions with the MoBni1 nucleator, after which it creates polarized actin cable bundles by association with F-actin and a concurrent inhibition of cofilin-mediated F-actin depolymerization. MoSPA2 mutants exhibit impaired hyphal growth and a reduced ability to infect host plants, underling the significance of this scaffolder. Overall, this work elucidates the fundamental mechanisms underlying fungal morphogenesis, offering the potential for targeted interventions in pathogenesis. Pathogenic fungal Spa2 condenses and activates actin regulators at the hyphal tip within the Spitzenk & ouml;rper, enabling polarized actin cable formation for filamentous growth and plant infection.
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| GB/T 7714 | He, Danxia , Li, Yuanbao , Ma, Qianqian et al. The phase-separating Magnaporthe oryzae MoSpa2 complex organizes actin nucleation centers for plant infection [J]. | PLANT CELL , 2025 , 37 (5) . |
| MLA | He, Danxia et al. "The phase-separating Magnaporthe oryzae MoSpa2 complex organizes actin nucleation centers for plant infection" . | PLANT CELL 37 . 5 (2025) . |
| APA | He, Danxia , Li, Yuanbao , Ma, Qianqian , Han, Libo , Tang, Dingzhong , Miao, Yansong . The phase-separating Magnaporthe oryzae MoSpa2 complex organizes actin nucleation centers for plant infection . | PLANT CELL , 2025 , 37 (5) . |
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Abstract ：
Rice blast disease caused by Magnaporthe oryzae poses a serious threat to rice security worldwide. This filamentous pathogen modulates rice defense responses by secreting effectors to facilitate infection. The phytohormone jasmonic acid (JA) plays crucial roles in the response to rice blast fungus. However, how M. oryzae disrupts JA-mediated resistance in rice is not well understood. In this study, we identify a new effector, a chloroplast-targeting protein (MoCHT1), from M. oryzae. Knocking out MoCHT1 decreases virulence, whereas heterologous expression of MoCHT1 in rice compromises disease resistance. MoCHT1 interacts with a rice LESION AND LAMINA BENDING (OsLLB) protein, a negative regulator of JA biosynthesis in the chloroplast. Loss-of-function of OsLLB leads to increased JA accumulation, thereby improving resistance to rice blast. The interaction between MoCHT1 and OsLLB results in the inhibition of OsLLB degradation, consequently reducing JA accumulation, thereby impairing JA content and decreasing plant disease resistance. Overall, this study reveals the molecular mechanism by which M. oryzae utilizes MoCHT1 to subvert rice JA signaling, broadening our understanding of how pathogens circumvent host immune responses by manipulating plant defense hormone biosynthesis. Copyright (c) 2025, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, and Genetics Society of China. Published by Elsevier Limited and Science Press. All rights are reserved, including those for text and data mining, AI training, and similar technologies.
Keyword ：
Chloroplast Chloroplast Effector Effector Jasmonic acid Jasmonic acid Plant defense response Plant defense response Rice blast Rice blast
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| GB/T 7714 | Shen, Ningning , Lu, Chuner , Wen, Yanhong et al. The Magnaporthe oryzae effector MoCHT1 targets and stabilizes rice OsLLB to suppress jasmonic acid synthesis and enhance infection [J]. | JOURNAL OF GENETICS AND GENOMICS , 2025 , 52 (11) : 1387-1400 . |
| MLA | Shen, Ningning et al. "The Magnaporthe oryzae effector MoCHT1 targets and stabilizes rice OsLLB to suppress jasmonic acid synthesis and enhance infection" . | JOURNAL OF GENETICS AND GENOMICS 52 . 11 (2025) : 1387-1400 . |
| APA | Shen, Ningning , Lu, Chuner , Wen, Yanhong , Deng, Boqian , Dong, Yu , Gong, Xiaojun et al. The Magnaporthe oryzae effector MoCHT1 targets and stabilizes rice OsLLB to suppress jasmonic acid synthesis and enhance infection . | JOURNAL OF GENETICS AND GENOMICS , 2025 , 52 (11) , 1387-1400 . |
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Magnaporthe oryzae (M. oryzae) is a devastating hemibiotrophic pathogen. Its biotrophic invasive hyphae (IH) are enclosed in the extrainvasive hyphal membrane produced by plant cells, thus generating a front line of the battlefield between the pathogen and the host plants. In plants, defense-related complexes such as proteins, callose-rich materials and vesicles, are directionally secreted to this interface to confer defense responses, but the underlying molecular mechanism is poorly understood. In this study, we found that a Myosin gene, Myosin A1 (OsMYA1), contributed to rice defense. The OsMYA1 knockout mutant exhibited decreased resistance to M. oryzae infection. OsMYA1 localizes to the actin cytoskeleton and surrounds the IH of M. oryzae. OsMYA1 interacts with an exocyst subunit, OsExo70H1, and regulates its accumulation at the plasma membrane (PM) and pathogen-plant interface. Furthermore, OsExo70H1 interacted with the rice syntaxin of the plants121 protein (OsSyp121), and the distribution of OsSyp121 to the PM or the pathogen-plant interface was disrupted in both the OsMYA1 and OsExo70H1 mutants. Overall, these results not only reveal a new function of OsMYA1 in rice blast resistance, but also uncover a molecular mechanism by which plants regulate defense against M. oryzae by OsMYA1-initiated vesicle secretory pathway, which originates from the actin cytoskeleton to the PM.
Keyword ：
cytoskeleton cytoskeleton plant defense mechanism plant defense mechanism rice blast rice blast vesicle delivery vesicle delivery
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| GB/T 7714 | Li, Yuan-Bao , Liu, Chengyu , Shen, Ningning et al. The actin motor protein OsMYA1 associates with OsExo70H1 and contributes to rice secretory defense by modulating OsSyp121 distribution [J]. | JOURNAL OF INTEGRATIVE PLANT BIOLOGY , 2024 , 66 (9) : 2058-2075 . |
| MLA | Li, Yuan-Bao et al. "The actin motor protein OsMYA1 associates with OsExo70H1 and contributes to rice secretory defense by modulating OsSyp121 distribution" . | JOURNAL OF INTEGRATIVE PLANT BIOLOGY 66 . 9 (2024) : 2058-2075 . |
| APA | Li, Yuan-Bao , Liu, Chengyu , Shen, Ningning , Zhu, Shuai , Deng, Xianya , Liu, Zixuan et al. The actin motor protein OsMYA1 associates with OsExo70H1 and contributes to rice secretory defense by modulating OsSyp121 distribution . | JOURNAL OF INTEGRATIVE PLANT BIOLOGY , 2024 , 66 (9) , 2058-2075 . |
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The dynamic assembly of the actin cytoskeleton is vital for Magnaporthe oryzae development and host infection. The actin-related protein MoFim1 is a key factor for organizing the M. oryzae actin cytoskeleton. Currently, how MoFim1 is regulated in M. oryzae to precisely rearrange the actin cytoskeleton is unclear. In this study, we found that MoFim1 associates with the M. oryzae mitogen-activated protein (MAP) kinase Pmk1 to regulate actin assembly. MoFim1 directly interacted with Pmk1, and the phosphorylation level of MoFim1 was decreased in Delta pmk1, which led to a change in the subcellular distribution of MoFim1 in the hyphae of Delta pmk1. Moreover, the actin cytoskeleton was aberrantly organized at the hyphal tip in the Delta pmk1, which was similar to what was observed in the Delta mofim1 during hyphal growth. Furthermore, phosphorylation analysis revealed that Pmk1 could phosphorylate MoFim1 at serine 94. Loss of phosphorylation of MoFim1 at serine 94 decreased actin bundling activity. Additionally, the expression of the site mutant of MoFim1 S94D (in which serine 94 was replaced with aspartate to mimic phosphorylation) in Delta pmk1 could reverse the defects in actin organization and hyphal growth in Delta pmk1. It also partially rescues the formation of appressorium failure in Delta pmk1. Taken together, these findings suggest a regulatory mechanism in which Pmk1 phosphorylates MoFim1 to regulate the assembly of the actin cytoskeleton during hyphal development and pathogenesis.
Keyword ：
Actin cytoskeleton Actin cytoskeleton Fimbrin Fimbrin Magnaporthe oryzae Magnaporthe oryzae Pmk1 Pmk1
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| GB/T 7714 | Li, Yuan-Bao , Shen, Ningning , Deng, Xianya et al. Fimbrin associated with Pmk1 to regulate the actin assembly during Magnaporthe oryzae hyphal growth and infection [J]. | STRESS BIOLOGY , 2024 , 4 (1) . |
| MLA | Li, Yuan-Bao et al. "Fimbrin associated with Pmk1 to regulate the actin assembly during Magnaporthe oryzae hyphal growth and infection" . | STRESS BIOLOGY 4 . 1 (2024) . |
| APA | Li, Yuan-Bao , Shen, Ningning , Deng, Xianya , Liu, Zixuan , Zhu, Shuai , Liu, Chengyu et al. Fimbrin associated with Pmk1 to regulate the actin assembly during Magnaporthe oryzae hyphal growth and infection . | STRESS BIOLOGY , 2024 , 4 (1) . |
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Cytoskeletal microtubules (MTs) play crucial roles in many aspects of life processes in eukaryotic organisms. They dynamically assemble physiologically important MT arrays under different cell conditions. Currently, aspects of MT assembly underlying the development and pathogenesis of the model plant pathogenic fungus Magnaporthe oryzae (M. oryzae) are unclear. In this study, we characterized the MT plus end binding protein MoMal3 in M. oryzae. We found that knockout of MoMal3 results in defects in hyphal polar growth, appressorium-mediated host penetration and nucleus division. Using high-resolution live-cell imaging, we further found that the MoMal3 mutant assembled a rigid MT in parallel with the MT during hyphal polar growth, the cage-like network in the appressorium and the stick-like spindle in nuclear division. These aberrant MT organization patterns in the MoMal3 mutant impaired actin-based cell growth and host infection. Taken together, these findings showed that M. oryzae relies on MoMal3 to assemble elaborate MT arrays for growth and infection. The results also revealed the assembly mode of MTs in M. oryzae, indicating that MTs are pivotal for M. oryzae growth and host infection and may be new targets for devastating fungus control.
Keyword ：
dynamic assembly dynamic assembly infection mechanism infection mechanism Magnaporthe oryzae Magnaporthe oryzae microtubule cytoskeleton microtubule cytoskeleton microtubule plus end microtubule plus end nucleus division nucleus division rice blast rice blast
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| GB/T 7714 | Shen, Ningning , Han, Libo , Liu, Zixuan et al. The Microtubule End Binding Protein Mal3 Is Essential for the Dynamic Assembly of Microtubules during Magnaporthe oryzae Growth and Pathogenesis [J]. | INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES , 2024 , 25 (5) . |
| MLA | Shen, Ningning et al. "The Microtubule End Binding Protein Mal3 Is Essential for the Dynamic Assembly of Microtubules during Magnaporthe oryzae Growth and Pathogenesis" . | INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 25 . 5 (2024) . |
| APA | Shen, Ningning , Han, Libo , Liu, Zixuan , Deng, Xianya , Zhu, Shuai , Liu, Chengyu et al. The Microtubule End Binding Protein Mal3 Is Essential for the Dynamic Assembly of Microtubules during Magnaporthe oryzae Growth and Pathogenesis . | INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES , 2024 , 25 (5) . |
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本发明涉及水稻抗病育种领域，具体涉及一种水稻稻瘟病抗性相关基因OsMYA1及其应用。OsMYA1基因的核苷酸序列如SEQ ID NO.1所示，其编码的蛋白的氨基酸序列如SEQ ID NO.2所示。本发明首次发现并证明水稻OsMYA1基因在水稻抗稻瘟病反应中的正调控作用，通过基因工程方法提高OsMYA1基因的表达水平，可以显著的增强稻瘟病抗性。本发明可应用于提高水稻等相关农作物的抗性遗传改良。
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| GB/T 7714 | 唐定中 , 李元宝 , 韩利波 . 一种水稻稻瘟病抗性相关基因OsMYA1及其应用 : CN202410848035.4[P]. | 2024-06-27 . |
| MLA | 唐定中 et al. "一种水稻稻瘟病抗性相关基因OsMYA1及其应用" : CN202410848035.4. | 2024-06-27 . |
| APA | 唐定中 , 李元宝 , 韩利波 . 一种水稻稻瘟病抗性相关基因OsMYA1及其应用 : CN202410848035.4. | 2024-06-27 . |
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本发明涉及植物基因工程技术领域。具体是一个介导水稻稻瘟病抗性相关基因OsCAD2的克隆、功能验证及应用，首次发现并证明OsCAD2基因在水稻抗稻瘟病反应中的正调控作用，通过基因工程方法提高OsCAD2的表达水平，可以显著的增强稻瘟病抗性，而敲除OsCAD2则降低水稻的稻瘟病抗性，本发明可应用于提高水稻等相关农作物的抗性遗传改良。
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| GB/T 7714 | 唐定中 , 韩利波 , 刘成玉 et al. 一种水稻稻瘟病抗性相关基因OsCAD2及其应用 : CN202410812497.0[P]. | 2024-06-21 . |
| MLA | 唐定中 et al. "一种水稻稻瘟病抗性相关基因OsCAD2及其应用" : CN202410812497.0. | 2024-06-21 . |
| APA | 唐定中 , 韩利波 , 刘成玉 , 李元宝 . 一种水稻稻瘟病抗性相关基因OsCAD2及其应用 : CN202410812497.0. | 2024-06-21 . |
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LIM proteins are widely spread in various types of plant cells and play diversely crucial cellular roles through actin cytoskeleton assembly and gene expression regulation. Till now, it has not been clear whether LIM proteins function in plant pathogen defense. In this study, we characterized a LIM protein, GhWLIM1C, in upland cotton (Gossypium hirsutum). We found that GhWLIM1C could bind and bundle the actin cytoskeleton, and it contains two LIM domains (LIM1 and LIM2). Both the two domains could bind directly to the actin filaments. Moreover, the LIM2 domain additionally bundles the actin cytoskeleton, indicating that it possesses a different biochemical activity than LIM1. The expression of GhWLIM1C responds to the infection of the cotton fungal pathogen Verticillium dahliae (V. dahliae). Silencing of GhWLIM1C decreased cotton resistance to V. dahliae. These may be associated with the down regulated plant defense response, including the PR genes expression and ROS accumulation in the infected cotton plants. In all, these results provide new evidence that a plant LIM protein functions in plant pathogen resistance and the assembly of the actin cytoskeleton are closely related to the triggering of the plant defense response.
Keyword ：
actin cytoskeleton actin cytoskeleton cotton cotton defense response defense response LIM protein LIM protein V. dahliae V. dahliae
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| GB/T 7714 | Cao, Tingyan , Qin, Minghui , Zhu, Shuai et al. Silencing of a Cotton Actin-Binding Protein GhWLIM1C Decreases Resistance against Verticillium dahliae Infection [J]. | PLANTS-BASEL , 2022 , 11 (14) . |
| MLA | Cao, Tingyan et al. "Silencing of a Cotton Actin-Binding Protein GhWLIM1C Decreases Resistance against Verticillium dahliae Infection" . | PLANTS-BASEL 11 . 14 (2022) . |
| APA | Cao, Tingyan , Qin, Minghui , Zhu, Shuai , Li, Yuanbao . Silencing of a Cotton Actin-Binding Protein GhWLIM1C Decreases Resistance against Verticillium dahliae Infection . | PLANTS-BASEL , 2022 , 11 (14) . |
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