Molecular plant pathology最新文献

{"title":"Fusarium sacchari 14-3-3 Protein FsBmh1 Sequesters a Novel Elicitor FsEcm33 to Evade Host Immunity.","authors":"Yuejia Chen, Yuming Lin, Lixian Zhao, Gengzhong Cheng, Liuting Huang, Yueying Zhao, Zhien Wei, Yuanzhi Mao, Xiaoxi Feng, Xipu He, Baoshan Chen, Jisen Zhang, Ziting Yao, Chengwu Zou","doi":"10.1111/mpp.70309","DOIUrl":"10.1111/mpp.70309","url":null,"abstract":"<p><p>Fusarium sacchari, the causal agent of pokkah boeng disease (PBD), is a globally devastating pathogen of sugarcane that causes substantial economic losses. During infection, the fungus employs elicitors to induce necrosis in plant tissues, thereby enhancing pathogen fitness. However, the key elicitors in F. sacchari and the mechanism by which plants recognize them remain unclear. Here, we identified a predicted glycosylated phosphatidylinositol (GPI)-anchored protein FsEcm33 as an elicitor that activates plant immunity. FsEcm33 is perceived in the apoplast of Nicotiana benthamiana by the receptor-like protein NbRE02 and induces cell death in a manner that requires the co-receptors NbBAK1 and NbSOBIR1. Purified FsEcm33 triggers basal immune responses in N. benthamiana and enhances disease resistance in multiple plant species, including sugarcane, rice, wheat, and star anise. In F. sacchari, FsEcm33 localizes to the cell surface, where its recognition by the host limits pathogen colonization. Notably, FsEcm33 specifically interacts with a 14-3-3 protein, FsBmh1, which reduces its accumulation at the fungal cell surface, suggesting a spatial sequestration mechanism that helps F. sacchari evade host immunity. Together, these findings establish FsEcm33 as a cell-surface elicitor perceived by NbRE02 and reveal an evolutionary strategy in which FsBmh1 sequesters FsEcm33 to evade host recognition and facilitate infection in F. sacchari.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"27 7","pages":"e70309"},"PeriodicalIF":5.0,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13323574/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148369102","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":"Enhanced Rice Yellow Mottle Virus Resistance via CRISPR/Cas9-Targeted Mutagenesis of the Rice eIF(iso)4G Gene.","authors":"Antony Kigaru, Elijah M Ateka, Hanu R Pappu, Everlyne M Nganga, Rosemary Murori, Mary Esther Toili, Steven Runo","doi":"10.1111/mpp.70312","DOIUrl":"10.1111/mpp.70312","url":null,"abstract":"<p><p>Rice is a staple crop primarily recognised for its high content of carbohydrates and proteins. Rice yellow mottle disease (RYMD) is a destructive disease affecting rice fields in sub-Saharan Africa and is caused by the rice yellow mottle virus (RYMV). Development of virus-resistant genotypes is a highly recommended and effective approach to controlling RYMV. A genetic approach that exploits recessive mutations in susceptibility (S) genes may enhance resistance to the virus. Reports indicate that most rice genotypes grown in Kenya are vulnerable to RYMV infection. Genome editing has shown promise in enhancing agronomic traits in crops. We obtained enhanced resistance to RYMV in the Indica rice cv. IR2793-80-01 using the CRISPR-Cas9 system. The eIF(iso)4G susceptibility gene was targeted because natural mutations in this gene confer recessive resistance to RYMV. A Cas9-OseIF(iso)4G-gRNA-expressing vector targeting the eIF(iso)4G gene was introduced into rice calli via Agrobacterium-mediated transformation. Ten T₂ homozygous mutant plant lines were assessed for their reaction to RYMV, and infection was significantly reduced. There were no significant differences in the agronomic characteristics between the T₂ mutant lines and the wild-type plants. CRISPR/Cas9-mediated knockout alleles of the eIF(iso)4G gene conferred enhanced resistance to RYMV, which may be classified as partial. Findings underscore the need to embrace precise editing strategies, such as prime editing, to generate superior resistance alleles. Overall, the study provides an alternative resistance enhancement strategy that can create knockout resistance alleles that can be incorporated into breeding programmes for RYMV resistance.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"27 7","pages":"e70312"},"PeriodicalIF":5.0,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13373454/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148456383","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":"Global Crotonylome Profiling Identifies TaPRXIIB Crotonylation as a Modulator H₂O₂ Homeostasis in Wheat Resistance to Puccinia triticina.","authors":"Qipeng Wang, Rongna Wang, Tianjie Sun, Qian Wang, Jia Gu, Zelin Niu, Na Liu, Shengfang Han, Dongmei Wang","doi":"10.1111/mpp.70288","DOIUrl":"10.1111/mpp.70288","url":null,"abstract":"<p><p>Wheat food security is severely threatened by Puccinia triticina infection. Although lysine crotonylation (Kcr) plays pivotal roles in plant stress responses, its function and regulation in biotic stress remain largely unknown. In this study, we investigated Kcr levels in wheat upon P. triticina infection and found that elevated protein crotonylation enhances resistance to P. triticina. We first performed a global crotonylome profiling of wheat in response to P. triticina infection and identified 3333 quantifiable Kcr sites across 952 proteins. Kcr sites were preferentially flanked by aliphatic amino acids, suggesting a sequence preference for this modification. Functional enrichment and protein-protein interaction (PPI) analyses based on crotonylated differentially expressed proteins (DEPs) further highlighted a strong association between Kcr-modified antioxidant enzymes and stress response processes. Furthermore, we investigated the modification pattens of two antioxidant enzymes and confirmed that TaPRXIIB negatively regulates wheat resistance to P. triticina by modulating H₂O₂ homeostasis. We found that crotonylation at K172 of TaPRXIIB disrupts the hydrogen bond between H187 and its prosthetic group, thereby reducing its enzymatic activity. This study presented a global crotonylome profile of wheat in response to P. triticina infection and revealed that the Kcr of TaPRXIIB at K172 negatively regulates its enzymatic activity.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"27 7","pages":"e70288"},"PeriodicalIF":5.0,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13354946/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148422577","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":"To Beet or Not (Just) to Beet: Ecology, Virulence and Genomic Insights Into the Leaf Spot Disease Causative Pseudomonas syringae pv. aptata.","authors":"Ivan Nikolić, Iva Rosić, Olja Medić, Tamara Ranković, Marina Sokić, Tanja Berić, Jelena Lozo, Slaviša Stanković","doi":"10.1111/mpp.70306","DOIUrl":"10.1111/mpp.70306","url":null,"abstract":"<p><strong>Taxonomy: </strong>Kingdom Bacteria; Phylum Proteobacteria; Class Gammaproteobacteria; Family Pseudomonadaceae; Genus Pseudomonas; Species Pseudomonas syringae species complex, Genomospecies 1, Phylogroup 02b.</p><p><strong>Biology: </strong>Gram-negative, aerobic, motile, rod-shaped with polar flagella, oxidase negative, arginine dihydrolase negative, levan production positive, potato rot negative, tobacco hypersensitivity positive.</p><p><strong>Virulence factors: </strong>T3SEs, toxins (syringomycin, syringopeptin, syringolin, mangotoxin, tabtoxin).</p><p><strong>Disease symptoms: </strong>Pseudomonas syringae causes disease symptoms on beet leaves characterised as circular or irregular, dark-edged, white to light brown necrotic spots that merge and spread over the entire leaf surface. Young leaves become completely necrotic within 7 days after the first symptom appears.</p><p><strong>Host range: </strong>Reported disease incidence mainly occurs on beets and cucurbits in temperate regions. Greenhouse trials showed an extremely wide host range for the strains isolated from diseased beets, causing disease on plants from nine different families and 16 different plant species.</p><p><strong>Disease control: </strong>Preventive measures focus primarily on sanitary and cultural practices. Integrated control programmes benefit from the regular application of copper formulations. The susceptibility of sugar beet cultivars to leaf spot disease varies, but no cultivar is completely resistant to the pathogen. Biological control may involve beneficial bacteria that suppress pathogens via metabolites and resource competition or by inducing systemic resistance in beet plants.</p><p><strong>Useful websites: </strong>https://www.pseudosonseed.org/chenopods-diseases/; https://www.cabi.org/isc/datasheet/44993; https://www.ncbi.nlm.nih.gov/assembly/?term=pseudomonas%20syringae%20pv.%20aptata; https://www.uniprot.org/proteomes?query=pseudomonas%20syringae%20pv.%20aptata; https://pnwhandbooks.org/plantdisease/host-disease/beet-red-beta-vulgaris-bacterial-leaf-spot.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"27 7","pages":"e70306"},"PeriodicalIF":5.0,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13318929/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148361467","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":"Ralstonia pseudosolanacearum PhcQ Controls Quorum Sensing-Dependent Phenotypes by Binding PhcA and Maintaining Its Protein Stability.","authors":"Min Chen, Lili Luo, Huixin Yang, Liujie Hu, Tao Liang, Masayuki Tsuzuki, Yasufumi Hikichi, Kouhei Ohnishi, Tao Guo, Chengtao Li, Peng Li, Yong Zhang","doi":"10.1111/mpp.70308","DOIUrl":"10.1111/mpp.70308","url":null,"abstract":"<p><p>The quorum-sensing (QS) system plays a crucial role in regulating the virulence of the Ralstonia solanacearum species complex (RSSC). It is controlled by the phcBSR operon and phcA genes. PhcQ may contribute to the activation of PhcA and regulates the expression of QS-dependent genes. Here, we genetically demonstrate that PhcQ functions as a key component of the QS regulatory pathway by maintaining the protein stability of PhcA in R. pseudosolanacearum OE1-1. Deletion of phcQ significantly increased the expression of genes encoding the type III secretion system but decreased the expression of genes for the synthesis of exopolysaccharide, consistent with that of PhcA. The phcQ mutants exhibited enhanced growth at early stages and retained weak virulence on tobacco plants, although they are nonvirulent on tomato plants. Using an overexpression system, we positioned PhcQ downstream of PhcB and upstream of PhcA in the QS regulatory cascade. PhcQ did not affect phcA transcription, while proteomic analysis and western blot revealed that PhcQ maintains PhcA protein stability, with PhcA protein levels reduced to approximately 41% in phcQ mutants. Further structural analysis revealed a disordered tail within the C-terminus of PhcA that is dispensable for PhcA function yet critical for protein stability. Using bimolecular fluorescence complementation and GST pull-down assay, we demonstrated that PhcQ binds directly to PhcA both in vitro and in planta, and deletion of this C-terminus tail impaired their binding affinity. These findings reveal a novel regulatory mechanism where PhcQ binds to PhcA and maintains its protein stability to ensure proper QS-dependent gene regulation in RSSC.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"27 7","pages":"e70308"},"PeriodicalIF":5.0,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13320629/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148361497","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":"Extracellular Vesicles: Key Mediators of Bioactive Molecule Transport in Plant-Microbe Interactions.","authors":"Hang Gao, Liying Pan, Ao Chen, Xiaolong Xing, Qingbin Chen, Yayue Wang, Xuan Huang","doi":"10.1111/mpp.70314","DOIUrl":"10.1111/mpp.70314","url":null,"abstract":"<p><p>Extracellular vesicles (EVs) are nanoscale, lipid-bilayer particles released by cells, which transport a diverse array of bioactive cargo such as nucleic acids, proteins, lipids, and metabolites. There is growing evidence that EVs act as important mediators in the bidirectional exchange of biomolecules between plants and microbes, thereby playing essential roles in their interactions. Plant-derived EVs can deliver defence-related nucleic acids and proteins to fungal pathogens, suppressing their virulence. Conversely, microbial EVs transport virulence factors, such as pathogenicity-related nucleic acids and proteins, into plant cells to promote infection. Despite recent advancements, research into the functions of plant EVs continues to lag significantly behind that of animal systems. This review begins by summarizing the role of EVs in facilitating cross-kingdom communication through the transport of bioactive molecules between plants and microorganisms, a process crucial for plant-microbe interactions. We highlight emerging evidence and potential mechanisms of EVs in establishing beneficial symbioses. Subsequently, we explore the putative functions of EVs in the systemic transmission of immune signals within plants. Finally, we propose future research directions based on current knowledge. By synthesizing these insights, this review serves as a timely and comprehensive resource to facilitate future functional studies on EVs in the interface of plant-microbe interactions.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"27 7","pages":"e70314"},"PeriodicalIF":5.0,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13355006/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148422533","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":"OsMAPK6 Phosphorylates and Degrades OsCATA to Regulate H₂O₂ Homeostasis Conferring Resistance to Bacterial Blight in Rice.","authors":"Lihan Wang, Jie Chen, Guixin Yuan, Xingxun Liu, Wenqian Zhu, Jian Shi, Yingshuang Liu, Dan Chen, Meng Yuan","doi":"10.1111/mpp.70313","DOIUrl":"10.1111/mpp.70313","url":null,"abstract":"<p><p>Mitogen-activated protein kinase (MAPK) cascades have been extensively reported to be involved in biotic and abiotic stress processes by regulating hydrogen peroxide (H₂O₂) homeostasis in plants. However, the detailed mechanisms by which MAPK cascades regulate H₂O₂ homeostasis in response to bacterial pathogens in rice remain largely unknown. Here, we demonstrate that rice CATALASE A (OsCATA) is a new substrate of OsMAPK6 and negatively regulates rice resistance to Xanthomonas oryzae pv. oryzae (Xoo) by directly suppressing H₂O₂ accumulation. Our results showed that OsMAPK6 interacts with OsCATA and specifically phosphorylates it at serine 460. The phosphorylation of OsCATA by OsMAPK6 attenuates OsCATA accumulation and reduces its catalase activity in vitro. The OsMAPK6-overexpressing (OsMAPK6-OE) plants showed lower catalase activity and higher accumulation of H₂O₂ compared with wild-type plants. The oscata mutant plants generated by the clustered regularly interspaced short palindromic repeats (CRISPR)/CRISPR-associated protein 9 (Cas9) strategy showed higher accumulation of H₂O₂ and increased resistance to Xoo. Together, these results suggest that the OsMAPK6-OsCATA module is involved in modulating rice H₂O₂ homeostasis and immunity.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"27 7","pages":"e70313"},"PeriodicalIF":5.0,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13329675/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148376370","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":"Both Conserved Aromatic Nature and Critical RNA Motif of Residue 67 in the ToBRFV Movement Protein May Be Essential for Evading Tm-2²-Mediated Resistance.","authors":"Yuhong Zhang, Jiayi Liu, Junchen Xu, Yuxin Nie, Luyou Wang, Fei Yan, Jianping Chen, Jian Wu","doi":"10.1111/mpp.70290","DOIUrl":"10.1111/mpp.70290","url":null,"abstract":"<p><p>The 68th amino acid residue (cysteine, C68) in tobacco mosaic virus (TMV) movement protein (MP) and the corresponding position in some tobamoviruses are required to trigger Tm-2²-mediated resistance. In contrast, the 67th amino acid residue (histidine, H67) in tomato brown rugose fruit virus (ToBRFV) MP enables evasion, although its key property remains unclear. To assess the key property of this site, a saturated mutant pool was generated at ToBRFV MP H67 and TMV MP C68, along with two single mutants, H67C and C68H. Infection assays were conducted using two tomato cultivars, Jingpeng No. 1 (JP, Tm-2²/tm-2) and Rutgers (RG, tm-2/tm-2), as well as wild-type (WT) and Tm-2² transgenic Nicotiana benthamiana. Progeny sequencing revealed species- and cultivar-specific outcomes. The mutants TAC and TAT (encoding the aromatic amino acid tyrosine, Y) and CAC (encoding the WT histidine, H), were the only ones detected in JP tomato and Tm-2² N. benthamiana. In single-infection assays, ToBRFV carrying TTC (encoding phenylalanine, F) at this position infected JP tomato, TAC (Y) enabled infection of Tm-2² N. benthamiana. TGG (encoding tryptophan, W) infected both JP tomato and Tm-2² N. benthamiana. Moreover, CAT (H) but not CAC (H), and TTC (F) but not TTT (F) infected JP plants, highlighting the role of the critical RNA motif. This suggests that the aromatic moiety and critical RNA motif at this position are essential for evading Tm-2²-mediated resistance, as the imidazole ring of the WT histidine also exhibits aromatic character. Therefore, Tm-2² may be engineered to recognize aromatic amino acids at this position to confer resistance to ToBRFV.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"27 7","pages":"e70290"},"PeriodicalIF":5.0,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13357992/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148430655","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":"An RLP23/Cf-9^TM-IC Chimeric Receptor Enhances nlp24-Triggered Immunity and Resistance to Phytophthora nicotianae in Nicotiana benthamiana.","authors":"Xiaodie Huo, Siying Pan, Hongju Xiao, Ling Wu, Lichi Zhong, Qiang Cheng","doi":"10.1111/mpp.70307","DOIUrl":"10.1111/mpp.70307","url":null,"abstract":"<p><p>Receptor-like protein AtRLP23 from Arabidopsis thaliana perceives the conserved microbial peptide nlp24 derived from necrosis- and ethylene-inducing peptide 1-like proteins (NLPs), but immune outputs are often weak in heterologous systems. Here, we engineered RLP23/Cf-9 chimeric receptors by fusing the extracellular domain of AtRLP23 to either the Cf-9 intracellular region (IC) or the Cf-9 transmembrane-intracellular region (TM-IC), and assessed their activity in Nicotiana benthamiana. In transient expression assays, AtRLP23 alone did not trigger hypersensitive cell death after infiltration with 10 μM nlp24, whereas both chimeras conferred nlp24-induced cell death, with RLP23/Cf-9^TM-IC producing markedly stronger macroscopic symptoms than RLP23/Cf-9^IC. Stable transgenic N. benthamiana expressing an untagged RLP23/Cf-9^TM-IC chimera showed enhanced nlp24 responsiveness, including stronger seedling growth inhibition and cell death after repeated 10 μM nlp24 treatment. In these plants, virus-induced gene silencing showed that chimera-mediated cell death requires SOBIR1 and the helper NLR NRC3, and transient NRC3 expression further sensitized the response, enabling cell death after a single 0.1 μM nlp24 treatment. In addition, the chimera significantly enhanced resistance to the oomycete Phytophthora nicotianae. Together, these results identify RLP23/Cf-9^TM-IC as an effective chimeric receptor and reveal transient NRC3 expression as a practical step to further potentiate nlp24-triggered output in N. benthamiana.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"27 7","pages":"e70307"},"PeriodicalIF":5.0,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13315810/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148352492","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":"Selective Autophagy Receptor CsNBR1 Confers Citrus Huanglongbing Resistance by Degrading 'Candidatus Liberibacter Asiaticus' Virulence Effectors.","authors":"Yaqian Shi, Xuejin Cui, Fang Fang, Zaiyu Yang, Yalin Mei, Shimian Ma, Changyong Zhou, Xuefeng Wang","doi":"10.1111/mpp.70310","DOIUrl":"10.1111/mpp.70310","url":null,"abstract":"<p><p>The selective autophagy receptor NEIGHBOUR OF BRCA1 (NBR1) is a key regulator of plant immunity, but its role against bacterial pathogens remains poorly understood. Here, we demonstrated that overexpression of CsNBR1 confers citrus resistance to huanglongbing (HLB) caused by 'Candidatus Liberibacter asiaticus' (CLas). CsNBR1 can interact with multiple virulence effector proteins of CLas, including SDE5115, SDE1, SDE19 and SDE5, leading to their degradation via the autophagic pathway. In addition, expression of CsNBR1 in Nicotiana benthamiana mitigated the leaf curling and dwarfing phenotypes triggered by SDE1 by reducing the protein content of SDE1. These findings reveal that CsNBR1 positively regulates citrus defence against CLas by degrading its effector proteins via selective autophagy, providing both mechanistic insights and a potential target for resistance breeding.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"27 7","pages":"e70310"},"PeriodicalIF":5.0,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13315814/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148352507","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}