Hao Sun, Malgorzata Ciska, Mongia Makki, Francisco Tenllado, Tomás Canto
{"title":"Adaptive substitutions at two amino acids of HCPro modify its functional properties to separately increase the virulence of a potyviral chimera.","authors":"Hao Sun, Malgorzata Ciska, Mongia Makki, Francisco Tenllado, Tomás Canto","doi":"10.1111/mpp.13487","DOIUrl":"10.1111/mpp.13487","url":null,"abstract":"<p><p>We had previously reported that a plum pox virus (PPV)-based chimera that had its P1-HCPro bi-cistron replaced by a modified one from potato virus Y (PVY) increased its virulence in some Nicotiana benthamiana plants, after mechanical passages. This correlated with the natural acquisition of amino acid substitutions in several proteins, including in HCPro at either position 352 (Ile→Thr) or 454 (Leu→Arg), or of mutations in non-coding regions. Thr in position 352 is not found among natural potyviruses, while Arg in 454 is a reversion to the native PVY HCPro amino acid. We show here that both mutations separately contributed to the increased virulence observed in the passaged chimeras that acquired them, and that Thr in position 352 is no intragenic suppressor to a Leu in position 454, because their combined effects were cumulative. We demonstrate that Arg in position 454 improved HCPro autocatalytic cleavage, while Thr in position 352 increased its accumulation and the silencing suppression of a reporter in agropatch assays. We assessed infection by four cloned chimera variants expressing HCPro with none of the two substitutions, one of them or both, in wild-type versus DCL2/4-silenced transgenic plants. We found that during infection, the transgenic context of altered small RNAs affected the accumulation of the four HCPro variants differently and hence, also infection virulence.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"25 6","pages":"e13487"},"PeriodicalIF":4.8,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11178974/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141321246","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":"Positive roles of the Ca<sup>2+</sup> sensors GbCML45 and GbCML50 in improving cotton Verticillium wilt resistance.","authors":"Feifei Yi, Yuzhe Li, Aosong Song, Xinying Shi, Shanci Hu, Shuang Wu, Lili Shao, Zongyan Chu, Kun Xu, Liangliang Li, Lam-Son Phan Tran, Weiqiang Li, Yingfan Cai","doi":"10.1111/mpp.13483","DOIUrl":"10.1111/mpp.13483","url":null,"abstract":"<p><p>As a universal second messenger, cytosolic calcium (Ca<sup>2+</sup>) functions in multifaceted intracellular processes, including growth, development and responses to biotic/abiotic stresses in plant. The plant-specific Ca<sup>2+</sup> sensors, calmodulin and calmodulin-like (CML) proteins, function as members of the second-messenger system to transfer Ca<sup>2+</sup> signal into downstream responses. However, the functions of CMLs in the responses of cotton (Gossypium spp.) after Verticillium dahliae infection, which causes the serious vascular disease Verticillium wilt, remain elusive. Here, we discovered that the expression level of GbCML45 was promoted after V. dahliae infection in roots of cotton, suggesting its potential role in Verticillium wilt resistance. We found that knockdown of GbCML45 in cotton plants decreased resistance while overexpression of GbCML45 in Arabidopsis thaliana plants enhanced resistance to V. dahliae infection. Furthermore, there was physiological interaction between GbCML45 and its close homologue GbCML50 by using yeast two-hybrid and bimolecular fluorescence assays, and both proteins enhanced cotton resistance to V. dahliae infection in a Ca<sup>2+</sup>-dependent way in a knockdown study. Detailed investigations indicated that several defence-related pathways, including salicylic acid, ethylene, reactive oxygen species and nitric oxide signalling pathways, as well as accumulations of lignin and callose, are responsible for GbCML45- and GbCML50-modulated V. dahliae resistance in cotton. These results collectively indicated that GbCML45 and GbCML50 act as positive regulators to improve cotton Verticillium wilt resistance, providing potential targets for exploitation of improved Verticillium wilt-tolerant cotton cultivars by genetic engineering and molecular breeding.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"25 6","pages":"e13483"},"PeriodicalIF":4.9,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11146148/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141199202","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":"ZmmiR398b negatively regulates maize resistance to sugarcane mosaic virus infection by targeting ZmCSD2/4/9","authors":"Xinran Gao, Zhichao Du, Kaiqiang Hao, Sijia Zhang, Jian Li, Jinxiu Guo, Zhiping Wang, Shixue Zhao, Lijun Sang, Mengnan An, Zihao Xia, Yuanhua Wu","doi":"10.1111/mpp.13462","DOIUrl":"https://doi.org/10.1111/mpp.13462","url":null,"abstract":"MicroRNAs (miRNAs) are widely involved in various biological processes of plants and contribute to plant resistance against various pathogens. In this study, upon sugarcane mosaic virus (SCMV) infection, the accumulation of maize (<jats:italic>Zea mays</jats:italic>) miR398b (ZmmiR398b) was significantly reduced in resistant inbred line Chang7‐2, while it was increased in susceptible inbred line Mo17. Degradome sequencing analysis coupled with transient co‐expression assays revealed that ZmmiR398b can target <jats:italic>Cu/Zn‐superoxidase dismutase2</jats:italic> (<jats:italic>ZmCSD2</jats:italic>), <jats:italic>ZmCSD4</jats:italic>, and <jats:italic>ZmCSD9</jats:italic> in vivo, of which the expression levels were all upregulated by SCMV infection in Chang7‐2 and Mo17. Moreover, overexpressing <jats:italic>ZmmiR398b</jats:italic> (OE398b) exhibited increased susceptibility to SCMV infection, probably by increasing reactive oxygen species (ROS) accumulation, which were consistent with <jats:italic>ZmCSD2/4/9</jats:italic>‐silenced maize plants. By contrast, silencing <jats:italic>ZmmiR398b</jats:italic> (STTM398b) through short tandem target mimic (STTM) technology enhanced maize resistance to SCMV infection and decreased ROS levels. Interestingly, copper (Cu)‐gradient hydroponic experiments demonstrated that Cu deficiency promoted SCMV infection while Cu sufficiency inhibited SCMV infection by regulating accumulations of ZmmiR398b and <jats:italic>ZmCSD2/4/9</jats:italic> in maize. These results revealed that manipulating the ZmmiR398b<jats:italic>‐ZmCSD2/4/9‐</jats:italic>ROS module provides a prospective strategy for developing SCMV‐tolerant maize varieties.","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"69 1","pages":""},"PeriodicalIF":4.9,"publicationDate":"2024-05-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140842303","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Louisa Wirtz, Florencia Casanova, Ulrich Schaffrath, Alex Wegner
{"title":"Development of a telomere vector‐based approach to overcome limitations caused by lethal phenotypes in the study of essential genes in Magnaporthe oryzae","authors":"Louisa Wirtz, Florencia Casanova, Ulrich Schaffrath, Alex Wegner","doi":"10.1111/mpp.13460","DOIUrl":"https://doi.org/10.1111/mpp.13460","url":null,"abstract":"Reverse genetic approaches are common tools in genomics for elucidating gene functions, involving techniques such as gene deletion followed by screening for aberrant phenotypes. If the generation of gene deletion mutants fails, the question arises whether the failure stems from technical issues or because the gene of interest (GOI) is essential, meaning that the deletion causes lethality. In this report, we introduce a novel method for assessing gene essentiality using the phytopathogenic ascomycete <jats:italic>Magnaporthe oryzae</jats:italic>. The method is based on the observation that telomere vectors are lost in transformants during cultivation without selection pressure. We tested the hypothesis that essential genes can be identified in deletion mutants co‐transformed with a telomere vector. The <jats:italic>M. oryzae</jats:italic> gene <jats:italic>MoPKC</jats:italic>, described in literature as essential, was chosen as GOI. Using CRISPR/Cas9 technology transformants with deleted GOI were generated and backed up by a telomere vector carrying a copy of the GOI and conferring fenhexamid resistance. Transformants in which the GOI deletion in the genome was not successful lost the telomere vector on media without fenhexamid. In contrast, transformants with confirmed GOI deletion retained the telomere vector even in absence of fenhexamid selection. In the latter case, the maintenance of the telomere indicates that the GOI is essential for the surveillance of the fungi, as it would have been lost otherwise. The method presented here allows to test for essentiality of genes when no mutants can be obtained from gene deletion approaches, thereby expanding the toolbox for studying gene function in ascomycetes.","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"91 1","pages":""},"PeriodicalIF":4.9,"publicationDate":"2024-05-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140842465","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Ming Ma, Liguang Tang, Rui Sun, Xueliang Lyu, Jiatao Xie, Yanping Fu, Bo Li, Tao Chen, Yang Lin, Xiao Yu, Weidong Chen, Daohong Jiang, Jiasen Cheng
{"title":"An effector SsCVNH promotes the virulence of Sclerotinia sclerotiorum through targeting class III peroxidase AtPRX71","authors":"Ming Ma, Liguang Tang, Rui Sun, Xueliang Lyu, Jiatao Xie, Yanping Fu, Bo Li, Tao Chen, Yang Lin, Xiao Yu, Weidong Chen, Daohong Jiang, Jiasen Cheng","doi":"10.1111/mpp.13464","DOIUrl":"https://doi.org/10.1111/mpp.13464","url":null,"abstract":"Many plant pathogens secrete effector proteins into the host plant to suppress host immunity and facilitate pathogen colonization. The necrotrophic pathogen <jats:italic>Sclerotinia sclerotiorum</jats:italic> causes severe plant diseases and results in enormous economic losses, in which secreted proteins play a crucial role. SsCVNH was previously reported as a secreted protein, and its expression is significantly upregulated at 3 h after inoculation on the host plant. Here, we further demonstrated that deletion of <jats:italic>SsCVNH</jats:italic> leads to attenuated virulence. Heterologous expression of <jats:italic>SsCVNH</jats:italic> in <jats:italic>Arabidopsis</jats:italic> enhanced pathogen infection, inhibited the host PAMP‐triggered immunity (PTI) response and increased plant susceptibility to <jats:italic>S. sclerotiorum</jats:italic>. SsCVNH interacted with class III peroxidase AtPRX71, a positive regulator of innate immunity against plant pathogens. SsCVNH could also interact with other class III peroxidases, thus reducing peroxidase activity and suppressing plant immunity. Our results reveal a new infection strategy employed by <jats:italic>S. sclerotiorum</jats:italic> in which the fungus suppresses the function of class III peroxidases, the major component of PTI to promote its own infection.","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"24 1","pages":""},"PeriodicalIF":4.9,"publicationDate":"2024-05-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140842128","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Tracy E. Hawk, Sarbottam Piya, Mst Shamira Sultana, Sobhan Bahrami Zadegan, Sarah Shipp, Nicole Coffey, Natalie B. McBride, John H. Rice, Tarek Hewezi
{"title":"Soybean MKK2 establishes intricate signalling pathways to regulate soybean response to cyst nematode infection","authors":"Tracy E. Hawk, Sarbottam Piya, Mst Shamira Sultana, Sobhan Bahrami Zadegan, Sarah Shipp, Nicole Coffey, Natalie B. McBride, John H. Rice, Tarek Hewezi","doi":"10.1111/mpp.13461","DOIUrl":"https://doi.org/10.1111/mpp.13461","url":null,"abstract":"Mitogen‐activated protein kinase (MPK) cascades play central signalling roles in plant immunity and stress response. The soybean orthologue of MPK kinase2 (GmMKK2) was recently identified as a potential signalling node whose expression is upregulated in the feeding site induced by soybean cyst nematode (SCN, <jats:italic>Heterodera glycines</jats:italic>). To investigate the role of GmMKK2 in soybean–SCN interactions, we overexpressed a catabolically inactive variant referred to as kinase‐dead variant (KD‐GmMKK2) using transgenic hairy roots. <jats:italic>KD‐GmMKK2</jats:italic> overexpression caused significant reduction in soybean susceptibility to SCN, while overexpression of the wild‐type variant (<jats:italic>WT‐GmMKK2</jats:italic>) exhibited no effect on susceptibility. Transcriptome analysis indicated that <jats:italic>KD‐GmMKK2</jats:italic> overexpressing plants are primed for SCN resistance via constitutive activation of defence signalling, particularly those related to chitin, respiratory burst, hydrogen peroxide and salicylic acid. Phosphoproteomic profiling of the <jats:italic>WT‐GmMKK2</jats:italic> and <jats:italic>KD‐GmMKK2</jats:italic> root samples upon SCN infection resulted in the identification of 391 potential targets of GmMKK2. These targets are involved in a broad range of biological processes, including defence signalling, vesicle fusion, chromatin remodelling and nuclear organization among others. Furthermore, GmMKK2 mediates phosphorylation of numerous transcriptional and translational regulators, pointing to the presence of signalling shortcuts besides the canonical MAPK cascades to initiate downstream signalling that eventually regulates gene expression and translation initiation. Finally, the functional requirement of specific phosphorylation sites for soybean response to SCN infection was validated by overexpressing phospho‐mimic and phospho‐dead variants of two differentially phosphorylated proteins SUN1 and IDD4. Together, our analyses identify GmMKK2 impacts on signalling modules that regulate soybean response to SCN infection.","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"36 1","pages":""},"PeriodicalIF":4.9,"publicationDate":"2024-05-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140833681","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Zizhang Li, Valeria Velásquez‐Zapata, J. Mitch Elmore, Xuan Li, Wenjun Xie, Sohini Deb, Xiao Tian, Sagnik Banerjee, Hans J. L. Jørgensen, Carsten Pedersen, Roger P. Wise, Hans Thordal‐Christensen
{"title":"Powdery mildew effectors AVRA1 and BEC1016 target the ER J‐domain protein HvERdj3B required for immunity in barley","authors":"Zizhang Li, Valeria Velásquez‐Zapata, J. Mitch Elmore, Xuan Li, Wenjun Xie, Sohini Deb, Xiao Tian, Sagnik Banerjee, Hans J. L. Jørgensen, Carsten Pedersen, Roger P. Wise, Hans Thordal‐Christensen","doi":"10.1111/mpp.13463","DOIUrl":"https://doi.org/10.1111/mpp.13463","url":null,"abstract":"The barley powdery mildew fungus, <jats:italic>Blumeria hordei</jats:italic> (Bh), secretes hundreds of candidate secreted effector proteins (CSEPs) to facilitate pathogen infection and colonization. One of these, CSEP0008, is directly recognized by the barley nucleotide‐binding leucine‐rich‐repeat (NLR) receptor MLA1 and therefore is designated AVR<jats:sub>A1</jats:sub>. Here, we show that AVR<jats:sub>A1</jats:sub> and the sequence‐unrelated Bh effector BEC1016 (CSEP0491) suppress immunity in barley. We used yeast two‐hybrid next‐generation interaction screens (Y2H‐NGIS), followed by binary Y2H and in planta protein–protein interactions studies, and identified a common barley target of AVR<jats:sub>A1</jats:sub> and BEC1016, the endoplasmic reticulum (ER)‐localized J‐domain protein <jats:italic>Hv</jats:italic>ERdj3B. Silencing of this ER quality control (ERQC) protein increased Bh penetration. <jats:italic>Hv</jats:italic>ERdj3B is ER luminal, and we showed using split GFP that AVR<jats:sub>A1</jats:sub> and BEC1016 translocate into the ER signal peptide‐independently. Overexpression of the two effectors impeded trafficking of a vacuolar marker through the ER; silencing of <jats:italic>Hv</jats:italic>ERdj3B also exhibited this same cellular phenotype, coinciding with the effectors targeting this ERQC component. Together, these results suggest that the barley innate immunity, preventing Bh entry into epidermal cells, requires ERQC. Here, the J‐domain protein <jats:italic>Hv</jats:italic>ERdj3B appears to be essential and can be regulated by AVR<jats:sub>A1</jats:sub> and BEC1016. Plant disease resistance often occurs upon direct or indirect recognition of pathogen effectors by host NLR receptors. Previous work has shown that AVR<jats:sub>A1</jats:sub> is directly recognized in the cytosol by the immune receptor MLA1. We speculate that the AVR<jats:sub>A1</jats:sub> J‐domain target being inside the ER, where it is inapproachable by NLRs, has forced the plant to evolve this challenging direct recognition.","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"10 1","pages":""},"PeriodicalIF":4.9,"publicationDate":"2024-05-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140833684","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"AtHVA22a, a plant-specific homologue of Reep/DP1/Yop1 family proteins is involved in turnip mosaic virus propagation.","authors":"Mingshuo Xue, Luc Sofer, Vincent Simon, Nathalie Arvy, Mamoudou Diop, Roxane Lion, Guillaume Beucher, Amandine Bordat, Jens Tilsner, Jean-Luc Gallois, Sylvie German-Retana","doi":"10.1111/mpp.13466","DOIUrl":"10.1111/mpp.13466","url":null,"abstract":"<p><p>The movement of potyviruses, the largest genus of single-stranded, positive-sense RNA viruses responsible for serious diseases in crops, is very complex. As potyviruses developed strategies to hijack the host secretory pathway and plasmodesmata (PD) for their transport, the goal of this study was to identify membrane and/or PD-proteins that interact with the 6K2 protein, a potyviral protein involved in replication and cell-to-cell movement of turnip mosaic virus (TuMV). Using split-ubiquitin membrane yeast two-hybrid assays, we screened an Arabidopsis cDNA library for interactors of <sup>TuMV</sup>6K2. We isolated AtHVA22a (Hordeum vulgare abscisic acid responsive gene 22), which belongs to a multigenic family of transmembrane proteins, homologous to Receptor expression-enhancing protein (Reep)/Deleted in polyposis (DP1)/Yop1 family proteins in animal and yeast. HVA22/DP1/Yop1 family genes are widely distributed in eukaryotes, but the role of HVA22 proteins in plants is still not well known, although proteomics analysis of PD fractions purified from Arabidopsis suspension cells showed that AtHVA22a is highly enriched in a PD proteome. We confirmed the interaction between <sup>TuMV</sup>6K2 and AtHVA22a in yeast, as well as in planta by using bimolecular fluorescence complementation and showed that <sup>TuMV</sup>6K2/AtHVA22a interaction occurs at the level of the viral replication compartment during TuMV infection. Finally, we showed that the propagation of TuMV is increased when AtHVA22a is overexpressed in planta but slowed down upon mutagenesis of AtHVA22a by CRISPR-Cas9. Altogether, our results indicate that AtHVA22a plays an agonistic effect on TuMV propagation and that the C-terminal tail of the protein is important in this process.</p>","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"25 5","pages":"e13466"},"PeriodicalIF":4.8,"publicationDate":"2024-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11104427/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141065455","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}
Xiaofei Liang, Wei Yu, Yanan Meng, Shengping Shang, Huanhuan Tian, Zhaohui Zhang, Jeffrey A. Rollins, Rong Zhang, Guangyu Sun
{"title":"Genome comparisons reveal accessory genes crucial for the evolution of apple Glomerella leaf spot pathogenicity in Colletotrichum fungi","authors":"Xiaofei Liang, Wei Yu, Yanan Meng, Shengping Shang, Huanhuan Tian, Zhaohui Zhang, Jeffrey A. Rollins, Rong Zhang, Guangyu Sun","doi":"10.1111/mpp.13454","DOIUrl":"https://doi.org/10.1111/mpp.13454","url":null,"abstract":"Apple Glomerella leaf spot (GLS) is an emerging fungal disease caused by <jats:italic>Colletotrichum fructicola</jats:italic> and other <jats:italic>Colletotrichum</jats:italic> species. These species are polyphyletic and it is currently unknown how these pathogens convergently evolved to infect apple. We generated chromosome‐level genome assemblies of a GLS‐adapted isolate and a non‐adapted isolate in <jats:italic>C. fructicola</jats:italic> using long‐read sequencing. Additionally, we resequenced 17 <jats:italic>C. fructicola</jats:italic> and <jats:italic>C. aenigma</jats:italic> isolates varying in GLS pathogenicity using short‐read sequencing. Genome comparisons revealed a conserved bipartite genome architecture involving minichromosomes (accessory chromosomes) shared by <jats:italic>C. fructicola</jats:italic> and other closely related species within the <jats:italic>C. gloeosporioides</jats:italic> species complex. Moreover, two repeat‐rich genomic regions (1.61 Mb in total) were specifically conserved among GLS‐pathogenic isolates in <jats:italic>C. fructicola</jats:italic> and <jats:italic>C. aenigma</jats:italic>. Single‐gene deletion of 10 accessory genes within the GLS‐specific regions of <jats:italic>C. fructicola</jats:italic> identified three that were essential for GLS pathogenicity. These genes encoded a putative non‐ribosomal peptide synthetase, a flavin‐binding monooxygenase and a small protein with unknown function. These results highlight the crucial role accessory genes play in the evolution of <jats:italic>Colletotrichum</jats:italic> pathogenicity and imply the significance of an unidentified secondary metabolite in GLS pathogenesis.","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"61 1","pages":""},"PeriodicalIF":4.9,"publicationDate":"2024-04-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140589337","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Qiushi Chen, Ya Li, Tianjiao Shen, Rong Wang, Meiling Su, Qiong Luo, Hua Shi, Guodong Lu, Zonghua Wang, Kevin G. Hardwick, Mo Wang
{"title":"Phosphorylation of Mad1 at serine 18 by Mps1 is required for the full virulence of rice blast fungus, Magnaporthe oryzae","authors":"Qiushi Chen, Ya Li, Tianjiao Shen, Rong Wang, Meiling Su, Qiong Luo, Hua Shi, Guodong Lu, Zonghua Wang, Kevin G. Hardwick, Mo Wang","doi":"10.1111/mpp.13456","DOIUrl":"https://doi.org/10.1111/mpp.13456","url":null,"abstract":"The spindle assembly checkpoint (SAC) proteins are conserved among eukaryotes safeguarding chromosome segregation fidelity during mitosis. However, their biological functions in plant‐pathogenic fungi remain largely unknown. In this study, we found that the SAC protein MoMad1 in rice blast fungus (<jats:italic>Magnaporthe oryzae</jats:italic>) localizes on the nuclear envelope and is dispensable for <jats:italic>M. oryzae</jats:italic> vegetative growth and tolerance to microtubule depolymerizing agent treatment. MoMad1 plays an important role in <jats:italic>M. oryzae</jats:italic> infection‐related development and pathogenicity. The monopolar spindle 1 homologue in <jats:italic>M. oryzae</jats:italic> (MoMps1) interacts with MoMad1 through its N‐terminal domain and phosphorylates MoMad1 at Ser‐18, which is conserved within the extended N termini of Mad1s from fungal plant pathogens. This phosphorylation is required for maintaining MoMad1 protein abundance and <jats:italic>M. oryzae</jats:italic> full virulence. Similar to the deletion of MoMad1, treatment with Mps1‐IN‐1 (an Mps1 inhibitor) caused compromised appressorium formation and decreased <jats:italic>M. oryzae</jats:italic> virulence, and these defects were dependent on its attenuating MoMad1 Ser‐18 phosphorylation. Therefore, our study indicates the function of Mad1 in rice blast fungal pathogenicity and sheds light on the potential of blocking Mad1 phosphorylation by Mps1 to control crop fungal diseases.","PeriodicalId":18763,"journal":{"name":"Molecular plant pathology","volume":"212 1","pages":""},"PeriodicalIF":4.9,"publicationDate":"2024-04-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140589336","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}