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学者姓名：韩利波
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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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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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Calcium (Ca2+) signaling plays a crucial role in plant immunity, regulating both pattern-triggered immunity (PTI) through cell-surface receptors and effector-triggered immunity (ETI) via intracellular nucleotide-binding, leucine-rich repeat receptors (NLRs). Calcium-dependent protein kinases (CPKs/CDPKs) serve as key Ca2+ sensors and signal transducers in these processes. In this study, we demonstrate the relevance of two rice CPKs, OsCPK5 and OsCPK13, for rice blast resistance. Both are Ca2+-responsive kinases, with potential in planta heteromer formation enhancing their phosphorylation/ signaling functions. Single oscpk5 and oscpk13 mutants exhibit impaired early PTI responses and enhanced susceptibility to rice blast fungus, suggesting that these kinases are essential for effective immunity. Surprisingly, although it is also defective in PTI, the oscpk5/13 double mutant displays enhanced resistance to rice blast. An NLR protein OsCPK5/13-ASSOCIATING RESISTANCE PROTEIN 1 (OsCARP1), which is physically associated with both OsCPK5 and OsCPK13, is genetically required for the heightened resistance of oscpk5/13. Furthermore, OsCARP1-induced cell death in Nicotiana benthamiana can be suppressed by the expression of OsCPK5 and OsCPK13. Based on these findings, we postulate that the positive blast resistance roles of OsCPK5 and OsCPK13 are guarded by OsCARP1, thus leading to OsCARP1-dependent ETI resistance in the oscpk5/13 double mutant or upon manipulation by still unknown pathogen effectors during infection. Our results offer insights into how plants counteract potential pathogen attack on key Ca2+ signaling immune components.
Keyword ：
Ca2+ Ca2+ cell death cell death NLR protein NLR protein OsCPK5 OsCPK5 rice blast resistance rice blast resistance
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| GB/T 7714 | Wang Zhanchun , Yu Shibo , Xu Wencai et al. Loss of calcium-dependent protein kinases OsCPK5 and OsCPK13 leads to NLR-dependent resistance in rice [J]. | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA , 2025 , 122 (45) . |
| MLA | Wang Zhanchun et al. "Loss of calcium-dependent protein kinases OsCPK5 and OsCPK13 leads to NLR-dependent resistance in rice" . | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 122 . 45 (2025) . |
| APA | Wang Zhanchun , Yu Shibo , Xu Wencai , Peng Han , Zhou Xuan , Liese Anja et al. Loss of calcium-dependent protein kinases OsCPK5 and OsCPK13 leads to NLR-dependent resistance in rice . | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA , 2025 , 122 (45) . |
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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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Gray blight disease (GBD) causes significant losses in tea production in China. Although genes and biological processes involved in resistance to fungal disease in tea plants have been identified, specific mechanisms of the GBD infection process remain unknown. In this study, morphological and multi-gene (TEF-TUB-ITS) phylogenetic characteristics were used to identify isolate CLBB1 of Pseudopestalotiopsis vietnamensis. Pathogenicity tests confirmed that isolate CLBB1 from tea leaves caused GBD in the susceptible tea cultivar Wuyi Rock (Camellia sinensis var. sinensis cv. Shuixian). Spores began to germinate 24 h after infection (hai), and after 48 h, elongated fungal hyphae formed from a single conidium. Transcriptome analysis revealed that 482, 517, and 369 genes were differentially expressed at 24, 48, and 72 hai, respectively, in Wuyi Rock tea leaves. Isolate CLBB1 infection elicited phenotype-related responses and activated defense-related pathways, including plant-pathogen interaction, MAPK signaling, and plant hormone signal transduction, suggesting a possible mechanism underlying phenotype-based susceptibility to CLBB1. Thus, a new Ps. vietnamensis strain causing GBD in the tea cultivar 'Shuixian' was discovered in this study. Transcriptome analysis indicated that pathogen invasion activated chitin-related MAPK pathways and that tea plants required a hormone to restrict CLBB1.
Keyword ：
Chitin-related MAPK pathways Chitin-related MAPK pathways gray blight disease gray blight disease Pseudopestalotiopsis Pseudopestalotiopsis tea tea transcriptional analysis transcriptional analysis
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| GB/T 7714 | Wu, Guangheng , Rui, Lu , Lu, Xiang et al. Characterization and Pathogenicity of Pseudopestalotiopsis vietnamensis Causing Gray Blight of Wuyi Rock Tea (Camellia sinensis) in China and Specific Mechanisms of Disease Infection [J]. | PHYTON-INTERNATIONAL JOURNAL OF EXPERIMENTAL BOTANY , 2023 , 92 (1) : 131-147 . |
| MLA | Wu, Guangheng et al. "Characterization and Pathogenicity of Pseudopestalotiopsis vietnamensis Causing Gray Blight of Wuyi Rock Tea (Camellia sinensis) in China and Specific Mechanisms of Disease Infection" . | PHYTON-INTERNATIONAL JOURNAL OF EXPERIMENTAL BOTANY 92 . 1 (2023) : 131-147 . |
| APA | Wu, Guangheng , Rui, Lu , Lu, Xiang , Han, Libo , Lv, Gan , Fu, Xianyu et al. Characterization and Pathogenicity of Pseudopestalotiopsis vietnamensis Causing Gray Blight of Wuyi Rock Tea (Camellia sinensis) in China and Specific Mechanisms of Disease Infection . | PHYTON-INTERNATIONAL JOURNAL OF EXPERIMENTAL BOTANY , 2023 , 92 (1) , 131-147 . |
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The devastating fungus Magnaporthe oryzae (M. oryzae) forms a specialized infection structure known as appressorium, which generates enormous turgor, to penetrate the plant cells. However, how M. oryzae regulates the appressorium turgor formation, is not well understood. In this study, we identified MoBZIP3, a bZIP transcription factor that functioned in pathogenesis in M. oryzae. We found that the pathogenicity of the MoBZIP3 knockout strain (Delta mobzip3) was significantly reduced, and the defect was restored after re-expression of MoBZIP3, indicating that MoBZIP3 is required for M. oryzae virulence. Further analysis showed that MoBZIP3 functions in utilization of glycogen and lipid droplets for generation of glycerol in appressorium. MoBZIP3 localized in the nucleus and could bind directly to the promoters of the glycerol synthesis-related genes, MoPTH2, MoTGL1 and MoPEX6, and regulate their expression which is critical for glycerol synthesis in the appressorium turgor pressure generation. Furthermore, the critical turgor sensor gene MoSln1 was also down regulated and its subcellular localization was aberrant in Delta mobzip3, which leads to a disordered actin assembly in the Delta mobzip3 appressorium. Taken together, these results revealed new regulatory functions of the bZIP transcription factor MoBZIP3, in regulating M. oryzae appressorium turgor formation and infection.
Keyword ：
appressorium turgor pressure appressorium turgor pressure Magnaporthe oryzae Magnaporthe oryzae transcription factor transcription factor virulence virulence
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| GB/T 7714 | Liu, Chengyu , Shen, Ningning , Zhang, Qian et al. Magnaporthe oryzae Transcription Factor MoBZIP3 Regulates Appressorium Turgor Pressure Formation during Pathogenesis [J]. | INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES , 2022 , 23 (2) . |
| MLA | Liu, Chengyu et al. "Magnaporthe oryzae Transcription Factor MoBZIP3 Regulates Appressorium Turgor Pressure Formation during Pathogenesis" . | INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 23 . 2 (2022) . |
| APA | Liu, Chengyu , Shen, Ningning , Zhang, Qian , Qin, Minghui , Cao, Tingyan , Zhu, Shuai et al. Magnaporthe oryzae Transcription Factor MoBZIP3 Regulates Appressorium Turgor Pressure Formation during Pathogenesis . | INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES , 2022 , 23 (2) . |
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Actin assembly at the hyphal tip is key for polar growth and pathogenesis of the rice blast fungus Magnaporthe oryzae. The mechanism of its precise assemblies and biological functions is not understood. Here, we characterized the role of M. oryzae Twinfilin (MoTwf) in M. oryzae infection through organizing the actin cables that connect to Spitzenkorper (Spk) at the hyphal tip. MoTwf could bind and bundle the actin filaments. It formed a complex with Myosin2 (MoMyo2) and the Woronin body protein Hexagonal peroxisome 1 (MoHex1). Enrichment of MoMyo2 and MoHex1 in the hyphal apical region was disrupted in a Delta Motwf loss-of-function mutant, which also showed a decrease in the number and width of actin cables. These findings indicate that MoTwf participates in the virulence of M. oryzae by organizing Spk-connected actin filaments and regulating MoHex1 distribution at the hyphal tip.
Keyword ：
actin cytoskeleton actin cytoskeleton Magnaporthe oryzae Magnaporthe oryzae plant fungal disease plant fungal disease
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| GB/T 7714 | Xu, Rui , Li, Yuan-Bao , Liu, Chengyu et al. Twinfilin regulates actin assembly and Hexagonal peroxisome 1 (Hex1) localization in the pathogenesis of rice blast fungus Magnaporthe oryzae [J]. | MOLECULAR PLANT PATHOLOGY , 2021 , 22 (12) : 1641-1655 . |
| MLA | Xu, Rui et al. "Twinfilin regulates actin assembly and Hexagonal peroxisome 1 (Hex1) localization in the pathogenesis of rice blast fungus Magnaporthe oryzae" . | MOLECULAR PLANT PATHOLOGY 22 . 12 (2021) : 1641-1655 . |
| APA | Xu, Rui , Li, Yuan-Bao , Liu, Chengyu , Shen, Ningning , Zhang, Qian , Cao, Tingyan et al. Twinfilin regulates actin assembly and Hexagonal peroxisome 1 (Hex1) localization in the pathogenesis of rice blast fungus Magnaporthe oryzae . | MOLECULAR PLANT PATHOLOGY , 2021 , 22 (12) , 1641-1655 . |
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