Molecular plant pathology最新文献

{"title":"The Small GTPase RHO1 Regulates ROS Homeostasis and Differentially Responds to Pathogens Infection via Interaction With Aquaporin TIP1;1 in Nicotiana.","authors":"Bowen Yuan, Chenglong Ji, Bolei Jiao, Yongchao Cheng, Zhiwei Jin, Jiale Jiang, Zeyi Xiao, Yong Liu, Jianmin Zeng, Cheng Yuan, Dehui Xi","doi":"10.1111/mpp.70333","DOIUrl":"10.1111/mpp.70333","url":null,"abstract":"<p><p>Small G-proteins are crucial regulators in plant growth and environmental responses. However, the mechanistic basis underlying their regulation of plant immunity to different pathogens is still poorly understood. Here, we showed that the small GTPase Ras homologous 1 (RHO1) responded differently to infection by distinct pathogens. Overexpression of RHO1 increased the plant susceptibility to chilli veinal mottle virus (ChiVMV) and necrotrophic Botrytis cinerea infections but enhanced plant resistance to the biotrophic bacterium Pseudomonas syringae. Further exploration revealed that there existed a direct interaction between RHO1 and tonoplast intrinsic protein 1;1 (TIP1;1), an aquaporin involved in water movement and the transport of hydrogen peroxide (H₂O₂) between vacuoles and cytoplasm. Under pathogen infection, the interaction between RHO1 and TIP1;1 could affect the distribution of reactive oxygen species (ROS) in the cytoplasm and vacuoles, promote the accumulation of ROS in the cytoplasm, leading to different responses of plant cells to pathogens with different lifestyles. Furthermore, the expression level of TIP1;1 was altered under infection by different pathogens. Our results demonstrate a mechanism by which the small GTPase RHO1 regulates ROS compartmentalization to affect the plant response to different pathogen infections, indicating the diversity of responses of a plant gene to different biotic factors.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"27 9","pages":"e70333"},"PeriodicalIF":5.0,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13525207/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148850946","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Tomato Yellow Leaf Curl Virus C4 Suppresses Antiviral Immunity by Targeting the 14-3-3 Protein SlTFT2.","authors":"Danna Gao, Feng Sun, Xiaoxiao Gao, Yinghua Ji, Yuelin Zhu","doi":"10.1111/mpp.70337","DOIUrl":"10.1111/mpp.70337","url":null,"abstract":"<p><p>Geminiviruses severely threaten global crop production. Tomato yellow leaf curl virus (TYLCV) encodes multifunctional effector C4, which participates in diverse biological processes and interacts with host proteins to facilitate infection. Despite extensive studies on geminiviral C4, how TYLCV C4 suppresses tomato immunity remains poorly characterized. In this study, we identified the tomato 14-3-3 protein SlTFT2 as a specific interaction partner of the TYLCV C4 protein. We demonstrated that SlTFT2 functions as a positive regulator of antiviral defence, as its silencing enhanced systemic viral infection, whereas its overexpression restricted infection. A critical serine residue at position 86 in C4 was essential for this interaction, and mutation of this residue (S86A or S86L) in TYLCV infectious clones significantly attenuated viral infectivity. Furthermore, C4, but not the S86A or S86L mutants, reduced the nuclear accumulation of SlTFT2. Collectively, our findings establish that the C4-SlTFT2 interaction is indispensable for TYLCV-mediated immunosuppression. Moreover, C4 promotes successful TYLCV infection by reducing the nuclear accumulation of SlTFT2 through this interaction, revealing a novel mechanism by which the virus subverts host defence by targeting a 14-3-3 protein.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"27 9","pages":"e70337"},"PeriodicalIF":5.0,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13530388/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148865671","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A Fungal Glycoside Hydrolase From Colletotrichum asianum Mini-Chromosomes Targets Host Chitinase to Suppress Plant Immunity.","authors":"Rui Wang, Tongtong Zhu, Rong Huang, Wenxiu Sun, Lihua Tang, Suiping Huang, Xiaolin Chen, Lu Zheng, Tom Hsiang, Qili Li","doi":"10.1111/mpp.70339","DOIUrl":"10.1111/mpp.70339","url":null,"abstract":"<p><p>Colletotrichum asianum, the cause of mango anthracnose, is a major threat to mango production worldwide. However, the mechanisms underlying plant invasion by C. asianum are poorly understood. Mini-chromosomes are increasingly recognised as indispensable components in the virulence of plant-pathogenic fungi. Here, we identify CaMutA, a secreted glycoside hydrolase 71 effector encoded on a mini-chromosome, as a critical pathogenicity factor that suppresses plant immune responses and is essential for infection by C. asianum. CaMutA directly interacts with the mango chitinase MiChi1. When heterologously expressed in Arabidopsis thaliana, MiChi1 confers enhanced resistance against multiple pathogens, suggesting its role in plant defence, a process that CaMutA subverts. Together, our findings uncover that a mini-chromosome-encoded effector can subvert plant immunity by directing the ubiquitin-mediated degradation of conserved defence-related chitinases. This study thus identifies promising targets for controlling mango anthracnose.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"27 9","pages":"e70339"},"PeriodicalIF":5.0,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13535142/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148875098","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"BcMFSR Is Required for Efficient Uptake of Exogenous dsRNA and Spray-Induced Gene Silencing in Botrytis cinerea.","authors":"Le Xu, Ze Yu, Ruonan Du, Huijie Ma, Xiaoxiao Hu, Ran Wei, Qiwang Hu, Cong Sheng, Wambui Doris Njoki, Pan Chen, Xuechao Shi, Cheng Tang, Huameng Zhang, Shaoxia Zhou, Haoming Zhong, Weishu Wang, Isashova Umida, Hongwei Zhao","doi":"10.1111/mpp.70343","DOIUrl":"10.1111/mpp.70343","url":null,"abstract":"<p><p>Spray-induced gene silencing (SIGS) uses exogenous double-stranded RNA (dsRNA) to suppress pathogen virulence or growth-related genes, offering a promising strategy for controlling grey mould caused by Botrytis cinerea at the gene level. In this study, we investigated the molecular mechanisms underlying the efficient uptake of dsRNAs by B. cinerea, making significant progress towards addressing key gaps in our understanding of SIGS. We identified four B. cinerea genes, BcBMP1, BcSOD1, BcGAR2, and BcVELB, as effective targets for grey mould control by employing an Arabidopsis thaliana SIGS screening system. Furthermore, by constructing a T-DNA insertion mutant library, we identified the ΔBcmfsR mutant, which exhibited significantly impaired dsRNA internalization. Functional assays revealed that the B. cinerea Major Facilitator Superfamily protein, BcMFSR, is critical for pH-dependent dsRNA uptake, facilitating SIGS efficacy. In the absence of functional BcMFSR, dsRNAs failed to reduce lesion size and B. cinerea virulence, regardless of the dsRNA sequence. BcMFSR is required for SIGS-mediated silencing of four genes. Moreover, fluorescent labelling confirmed the localization of both BcMFSR and dsRNA in vesicular structures within hyphae, suggesting its involvement in endocytosis. Our discoveries not only established the novel role of BcMFSR in RNA uptake but also provided a foundation for improving the efficiency of RNA pesticides and broadening their agricultural applications.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"27 9","pages":"e70343"},"PeriodicalIF":5.0,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13591111/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149012681","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Systematic Identification and Functional Characterisation of Colletotrichum fructicola Effectors During Camellia oleifera Colonisation.","authors":"Lingxue Cao, Wentong Dong, Kaile Sun, Xizhe Sun, Chenxue Song, Lisong Ma, Geng Meng","doi":"10.1111/mpp.70338","DOIUrl":"10.1111/mpp.70338","url":null,"abstract":"<p><p>Camellia oleifera is an important woody oil crop in southern China, but its production is severely threatened by anthracnose caused by Colletotrichum fructicola. C. fructicola deploys secreted effector proteins to establish infection. However, systematic identification and functional characterisation of C. fructicola effector genes upregulated during infection remains largely unexplored. Here, we integrated genome-wide secretome prediction with RNA-seq data from C. oleifera leaves inoculated with C. fructicola to identify candidate effectors induced during infection, followed by functional screening, targeted gene deletion, complementation and pathogenicity assays. Five novel effectors required for C. fructicola full virulence were identified, all of which suppressed Bax-induced cell death in Nicotiana benthamiana. Targeted deletion of the corresponding genes in C. fructicola reduced lesion areas by 47%-78% on C. oleifera leaves and by up to 67% on apple fruits, whereas complementation restored their virulence to wild-type levels. Transcriptomic profiling of infected postharvest C. oleifera fruits identified differentially expressed genes enriched in GO terms related to copper ion response, as well as in KEGG pathways associated with phenylpropanoid biosynthesis, taurine and hypotaurine metabolism, and plant-pathogen interactions. In addition, superoxide dismutase (SOD), catalase (CAT) and peroxidase (POD) activities, as well as malondialdehyde content, were altered in C. oleifera leaves inoculated with the effector-deletion mutants compared with those infected with the wild-type strain, suggesting that these effectors may contribute to the modulation of host oxidative stress responses. Taken together, our findings provide genetic and physiological evidence that these effectors contribute to C. fructicola virulence, offering potential targets for anthracnose control.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"27 9","pages":"e70338"},"PeriodicalIF":5.0,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13547971/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148900982","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Transcriptional and Functional Insights Into the All-Stage Resistance Gene GmRmd1-Mediated Regulation of Resistance to Powdery Mildew in Soybean.","authors":"Guoqiang Liu, Chen Ling, Tingting Xu, Xuehui Zhang, Jiacan Jiang, Xiaomin Xu, Lu Li, Jiajian Zhang, Bing Hu, Mengshi Liu, Yunxin He, Cunyi Yang","doi":"10.1111/mpp.70330","DOIUrl":"10.1111/mpp.70330","url":null,"abstract":"<p><p>Powdery mildew disease (PMD), caused by Microsphaera diffusa, is a devastating soybean foliar disease. This study identified GmRmd1 as a candidate in Guangxi landrace MSRF (all-stage resistance to PMD) and validated it as a positive PMD resistance regulator. Hypersensitive response (HR) assays confirmed its Toll interleukin-1 receptor (TIR), nucleotide-binding site (NBS) and basic secretory protein (BSP) domains are critical for immune responses. GmRmd1 was induced by M. diffusa, and its expression was inhibited by GmWRKY27 and GmERF138 specifically binding to the W-box and GCC-box elements of the GmRmd1 promoter, respectively. RNA-Seq revealed that chromosome 16 (chr16) resistance cluster genes (Glyma.16G214100, Glyma.16G214200, Glyma.16G215100 and Glyma.16G215800) showed GmRmd1-related expression patterns. Yeast two-hybrid, bimolecular fluorescence complementation and luciferase assays demonstrated GmRmd1 interacts not only with itself, but also with GmRmd2 (Glyma.16G215100), GmRmd3 (Glyma.16G214900) and GmRnl1 (NLR cofactor). In addition, mutants of GmRmd3 and GmRnl1 are more susceptible to M. diffusa. Notably, GmRmd1 enhances the resistance of PMD by interacting with GmPER1 (lignin synthesis-related) and increasing the synthesis of lignin. Genomic analysis indicated that the number of soybean accessions carrying the GmRmd1 locus gradually decreases from north to south and from west to east in China. Taken together, GmRmd1 forms functional protein complexes with GmRmd2, GmRmd3, and GmRnl1 to regulate lignin biosynthesis and thereby modulate disease resistance. These insights provide novel perspectives into the molecular mechanisms of GmRmd1-mediated resistance to soybean PMD.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"27 9","pages":"e70330"},"PeriodicalIF":5.0,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13525195/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148850902","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The ER-Golgi Lipid Exchanger PsORP1 Is Essential for Phytophthora sojae Development and Is Blocked by Oxathiapiprolin via Its OSBP-Related Domain (ORD).","authors":"Xiaofei Liu, Chengcheng Li, Guangda Shao, Qin Peng, Haixia Wang, Jianqiang Miao, Xili Liu","doi":"10.1111/mpp.70331","DOIUrl":"10.1111/mpp.70331","url":null,"abstract":"<p><p>Oxysterol-binding protein (OSBP)-related proteins (ORPs) are indispensable eukaryotic lipid transporters and promising targets for pharmaceutical and agrochemical exploitation. Among ORP family members across kingdoms, oomycete ORP1 constitutes a phylogenetically distinct subtype that evolved independently in oomycetes, which is markedly divergent from ORP homologues in animals, plants and fungi. Oxathiapiprolin, the first commercial fungicide targeting OSBP family proteins, specifically acts on oomycete ORP1 and exhibits robust inhibitory efficacy against diverse Phytophthora pathogens and downy mildews. Nevertheless, the molecular function of oomycete ORP1 and the inhibitory mechanism of oxathiapiprolin remain poorly defined. Here, we demonstrate that PsORP1 of Phytophthora sojae specifically localises to ER-Golgi membrane contact sites (MCSs) and is indispensable for vegetative growth and asexual/sexual development of P. sojae. In vitro liposome reconstitution assays confirmed that the conserved C-terminal OSBP-related domain (ORD) of PsORP1 mediates canonical phosphatidylserine (PS)/phosphatidylinositol 4-phosphate (PI4P) counter-transport. Biochemical binding assays further verified that oxathiapiprolin directly interacts with the ORD of PsORP1 and competitively blocks PS/PI4P lipid exchange. Collectively, this study demonstrates that PsORP1 localises to ER-Golgi MCSs and mediates ORD-dependent PS/PI4P counter-transport, which is essential for P. sojae development, and elucidates that oxathiapiprolin directly targets the ORD to competitively block this lipid exchange, providing a structural framework for rational design of next-generation OSBP-targeting inhibitors against oomycetes.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"27 9","pages":"e70331"},"PeriodicalIF":5.0,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13538951/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148880622","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Suppression of ZmJAZ12 Expression Modulates Jasmonic Acid and Salicylic Acid Signalling and Enhances Maize Resistance to Southern Corn Rust.","authors":"Jiarui Han, Qi Wang, Xiaopeng Sun, Zhijia Yu, Bingyang Li, Ziyu Wang, Chuang Zhang, Weilin Wu, Guan-Feng Wang, Gengshen Chen, Xiangguo Liu","doi":"10.1111/mpp.70349","DOIUrl":"10.1111/mpp.70349","url":null,"abstract":"<p><p>Southern corn rust (SCR), caused by the biotrophic fungus Puccinia polysora, severely threatens maize yield worldwide. In this study, we identified ZmJAZ12, a member of the JASMONATE ZIM-domain (JAZ) protein family, as a negative regulator of SCR resistance in maize. Genome-wide association study (GWAS) and expression analyses revealed that the expression level of ZmJAZ12 was negatively correlated with SCR resistance, and the resistant haplotypes exhibited significantly lower transcript abundance of ZmJAZ12. The ZmJAZ12 overexpression (OE) lines showed enhanced susceptibility to SCR, while ZmJAZ12 knockout mutants generated via CRISPR/Cas9-mediated gene editing were more resistant to SCR. Transcriptomic profiling revealed that downregulation of key genes in the salicylic acid (SA) and jasmonic acid (JA) pathways occurred in the OE lines. ZmJAZ12 interacted with ZmMYC5, a core transcription factor in the JA signalling cascade, forming a regulatory module that regulates hormonal signalling and immune responses. Collectively, these findings reveal that ZmJAZ12 acts as a susceptibility gene, providing evidence for the JA/SA signalling crosstalk mechanism in plant immunity. This study provides a potential genetic target for enhancing disease resistance in maize breeding.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"27 9","pages":"e70349"},"PeriodicalIF":5.0,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13615170/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149062812","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Functional Dissection of the Turnip Crinkle Virus Coat Protein Links ATG8 Association to Autophagy-Associated Antiviral Regulation.","authors":"Sung Hee Jo, Ju Yeon Moon, Sukyoung Jung, Gah-Hyun Lim, Pradeep Kachroo, Jeong Mee Park","doi":"10.1111/mpp.70350","DOIUrl":"10.1111/mpp.70350","url":null,"abstract":"<p><p>The coat protein (CP) of turnip crinkle virus (TCV) plays multifaceted roles in viral infection, acting as both an avirulence (Avr) factor recognized by the resistance protein HRT and a viral suppressor of RNA silencing (VSR). However, how these dual activities are coordinated remains unclear. Here, we demonstrate that the position of a fluorescent protein (FP) tag on CP functionally separates its two activities. C-terminal tagging (CP-GFP) preserved the ability to trigger HRT-dependent hypersensitive response (HR) but abolished silencing suppression, whereas N-terminal tagging (YFP-CP) retained VSR activity but failed to induce HR. These functional differences correlated with distinct subcellular localizations: Avr activity required both nuclear and cytoplasmic localization, while VSR function was confined to the cytoplasm. We further show that the N-terminal region of CP associates with autophagy-related protein 8 (ATG8), linking CP to autophagy-associated antiviral pathways. Autophagy-deficient atg5 and atg7 mutants exhibited enhanced susceptibility to TCV, supporting a role for autophagy in antiviral defence during infection. Together, our findings reveal that TCV CP contains spatially and mechanistically separable determinants for Avr and VSR functions and identify CP-ATG8 association as a potential interface between viral infection and host autophagy-associated regulation.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"27 9","pages":"e70350"},"PeriodicalIF":5.0,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13615169/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149062826","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"MgCBP1 Synergistically Enhances MgENG2-Mediated Cellulose Degradation to Promote Parasitism in Meloidogyne graminicola.","authors":"Chunhui Huang, Yuqing Cao, Ao Xu, Jiani Chen, Borong Lin, Qiuling Huang, Kan Zhuo","doi":"10.1111/mpp.70346","DOIUrl":"10.1111/mpp.70346","url":null,"abstract":"<p><p>Plant-parasitic nematodes secrete effector proteins, including cell wall-degrading enzymes (CWDEs) and cell wall-modifying proteins (CWMPs), to facilitate infection. However, whether cellulose-binding proteins (CBPs), which are a class of CWMPs, can synergize with cellulases (a subgroup of CWDEs) to promote parasitism remains unclear. Here, we identified and characterized a CBP (MgCBP1) and a β-1,4-endoglucanase (MgENG2) from the rice root-knot nematode Meloidogyne graminicola. MgCBP1 contains a conserved cellulose-binding module (CBM) and is specifically expressed in the subventral oesophageal glands, with transcript levels markedly up-regulated in pre-parasitic second-stage juveniles (pre-J2s) and during early infection. Recombinant MgCBP1 bound cellulose, disrupted fibre structure and enhanced cellulase-mediated hydrolysis via its intact CBM, whereas a CBM-disrupted mutant lack both activities. MgENG2, which lacks a CBM, exhibited strong endoglucanase activity and displayed an expression profile similar to that of MgCBP1. MgCBP1 significantly enhanced the hydrolytic efficiency of MgENG2, whereas its CBM-disrupted mutant did not. Transgenic rice overexpressing MgCBP1 showed enhanced susceptibility to M. graminicola. RNAi-mediated individual silencing of MgCBP1 or MgENG2 both reduced infection, with MgENG2 silencing showing a significantly greater effect. Co-silencing of both genes yielded the greatest reduction in gall formation and parasitic nematode numbers, which was significantly greater than that of MgCBP1-only silencing, but did not differ significantly from MgENG2-only silencing. Collectively, these findings demonstrate that MgCBP1 promotes nematode parasitism by binding cellulose, disrupting fibril surface integrity and enhancing the cellulolytic efficiency of MgENG2, providing the first experimental evidence that a CBP from a plant pathogen can synergistically facilitate infection by boosting endoglucanase-mediated cellulose degradation.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"27 9","pages":"e70346"},"PeriodicalIF":5.0,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13585997/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148990824","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}