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Gene deletion and constitutive expression of the pectate lyase gene 1 (MoPL1) lead to diminished virulence of Magnaporthe oryzae
Alex Wegner , Florencia Casanova , Marco Loehrer , Angelina Jordine , Stefan Bohnert , Xinyu Liu , Zhengguang Zhang , Ulrich Schaffrath
J. Microbiol. 2022;60(1):79-88.   Published online December 29, 2021
DOI: https://doi.org/10.1007/s12275-022-1074-7
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  • 14 Web of Science
  • 12 Crossref
AbstractAbstract
Phytopathogenic fungi are known to secrete specific proteins which act as virulence factors and promote host colonization. Some of them are enzymes with plant cell wall degradation capability, like pectate lyases (Pls). In this work, we examined the involvement of Pls in the infection process of Magnaporthe oryzae, the causal agent of rice blast disease. From three Plgenes annotated in the M. oryzae genome, only transcripts of MoPL1 considerably accumulated during the infection process with a peak at 72 h post inoculation. Both, gene deletion and a constitutive expression of MoPL1 in M. oryzae led to a significant reduction in virulence. By contrast, mutants that constitutively expressed an enzymatic inactive version of MoPl1 did not differ in virulence compared to the wild type isolate. This indicates that the enzymatic activity of MoPl1 is responsible for diminished virulence, which is presumably due to degradation products recognized as danger associated molecular patterns (DAMPs), which strengthen the plant immune response. Microscopic analysis of infection sites pointed to an increased plant defense response. Additionally, MoPl1 tagged with mRFP, and not the enzymatic inactive version, focally accumulated in attacked plant cells beneath appressoria and at sites where fungal hyphae transverse from one to another cell. These findings shed new light on the role of pectate lyases during tissue colonization in the necrotrophic stage of M. oryzae's life cycle.

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Citations to this article as recorded by  
  • Enhanced Resistance to Pokkah Boeng Disease in Sugarcane Through Host‐Induced Gene Silencing Targeting FsCYP51 in Fusarium sacchari
    Liuyu Yin, Zhen Huang, Yuming Zhou, Minyan Lu, Lixiang Zhu, Ruolin Di, Zhenzhen Duan, Yixue Bao, Qin Hu, Charles A. Powell, Baoshan Chen, Jisen Zhang, Muqing Zhang, Wei Yao
    Plant, Cell & Environment.2025;[Epub]     CrossRef
  • Fusarium sacchari FsNis1 induces plant immunity
    Ruolin Di, Lixiang Zhu, Zhen Huang, Minyan Lu, Liuyu Yin, Caixia Wang, Yixue Bao, Zhenzhen Duan, Charles A. Powell, Qin Hu, Jisen Zhang, Muqing Zhang, Wei Yao
    Gene.2024; 907: 148260.     CrossRef
  • Litchi aspartic protease LcAP1 enhances plant resistance via suppressing cell death triggered by the pectate lyase PlPeL8 from Peronophythora litchii
    Wen Li, Peng Li, Yizhen Deng, Zijing Zhang, Junjian Situ, Ji Huang, Minhui Li, Pinggen Xi, Zide Jiang, Guanghui Kong
    New Phytologist.2024; 242(6): 2682.     CrossRef
  • Unravelling transcriptional responses of the willow to Fusarium kuroshium infection
    Enrique Ibarra-Laclette, Luis A. Martínez-Rodríguez, Eric E. Hernández-Domínguez, Mizraim Olivares-Miranda, Benjamín Rodríguez-Haas, Emanuel Villafán, Claudia-Anahí Pérez-Torres, Diana Sánchez-Rangel
    Physiological and Molecular Plant Pathology.2024; 133: 102379.     CrossRef
  • Recognition of the inducible, secretory small protein OsSSP1 by the membrane receptor OsSSR1 and the co-receptor OsBAK1 confers rice resistance to the blast fungus
    Tianfeng Zhao, Shijie Ma, Ziying Kong, Haimiao Zhang, Yi Wang, Junzhe Wang, Jiazong Liu, Wanzhen Feng, Tong Liu, Chunyan Liu, Suochen Liang, Shilin Lu, Xinyu Li, Haipeng Zhao, Chongchong Lu, Muhammad Zunair Latif, Ziyi Yin, Yang Li, Xinhua Ding
    Molecular Plant.2024; 17(5): 807.     CrossRef
  • A plant cell death-inducing protein from litchi interacts with Peronophythora litchii pectate lyase and enhances plant resistance
    Wen Li, Peng Li, Yizhen Deng, Junjian Situ, Zhuoyuan He, Wenzhe Zhou, Minhui Li, Pinggen Xi, Xiangxiu Liang, Guanghui Kong, Zide Jiang
    Nature Communications.2024;[Epub]     CrossRef
  • Roles of Three FgPel Genes in the Development and Pathogenicity Regulation of Fusarium graminearum
    Lu Cai, Xiao Xu, Ye Dong, Yingying Jin, Younes M. Rashad, Dongfang Ma, Aiguo Gu
    Journal of Fungi.2024; 10(10): 666.     CrossRef
  • Pectate Lyase from Fusarium sacchari Induces Plant Immune Responses and Contributes to Virulence
    Caixia Wang, Zhen Huang, Zhenzhen Duan, Lixiang Zhu, Ruolin Di, Yixue Bao, Charles A. Powell, Qin Hu, Baoshan Chen, Muqing Zhang, Wei Yao, Lindsey Price Burbank
    Microbiology Spectrum.2023;[Epub]     CrossRef
  • Pectate Lyase Genes Abundantly Expressed During the Infection Regulate Morphological Development of Colletotrichum camelliae and CcPEL16 Is Required for Full Virulence to Tea Plants
    Hong Jiang, Qinghai Cao, Xinchao Wang, Wuyun Lv, Yuchun Wang, Aaron P. Mitchell
    mSphere.2023;[Epub]     CrossRef
  • Small GTPases RasA and RasB regulate development, patulin production, and virulence of Penicillium expansum
    Yuanyuan Zong, Xuemei Zhang, Di Gong, Feng Zhang, Lirong Yu, Yang Bi, Edward Sionov, Dov Prusky
    Postharvest Biology and Technology.2023; 197: 112192.     CrossRef
  • Whole-genome sequencing and comparative genomics reveal the potential pathogenic mechanism of Neoscytalidium dimidiatum on pitaya
    Meng Wang, Min Xu, Zhouwen Wang, Yi Ding, Shaoling Kang, Senrong Jiang, Shuangshuang Wei, Jun Xie, Jiaquan Huang, Dongdong Li, Wenbin Hu, Hongli Li, Xingyu Jiang, Hua Tang, Yonglin Wang
    Microbiology Spectrum.2023;[Epub]     CrossRef
  • Identification of RT-qPCR reference genes suitable for gene function studies in the pitaya canker disease pathogen Neoscytalidium dimidiatum
    Meng Wang, Zhouwen Wang, Shuangshuang Wei, Jun Xie, Jiaquan Huang, Dongdong Li, Wenbin Hu, Hongli Li, Hua Tang
    Scientific Reports.2022;[Epub]     CrossRef
Mutants defective in the production of encapsulin show a tan-phaselocked phenotype in Myxococcus xanthus
Dohee Kim , Juo Choi , Sunjin Lee , Hyesook Hyun , Kyoung Lee , Kyungyun Cho
J. Microbiol. 2019;57(9):795-802.   Published online June 11, 2019
DOI: https://doi.org/10.1007/s12275-019-8683-9
  • 45 View
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  • 13 Web of Science
  • 10 Crossref
AbstractAbstract
Myxococcus xanthus, a myxobacterium, displays phase variation between yellow phase and tan phase. We found that deletion of the encA gene encoding encapsulin and the encF gene encoding a metalloprotease causes formation of tan colonies that never transform into yellow colonies. The encA and encF mutants were defective in the production of DKxanthene and myxovirescin. They did not produce extracellular polysaccharides; hence, the cells did not aggregate in liquid and showed reduced swarming on agar plates. The mutants had defective sporulation, but were rescued extracellularly by wild type cells. All these traits indicate that the encA and encF mutants are likely to be tan-phase-locked, and encapsulin has a close relationship with phase variation in M. xanthus. The encA and encF genes are localized in the same gene cluster, encBAEFG (MXAN_3557~MXAN_3553). Unlike the encA and encF genes, deletion of other genes in the cluster did not show tan-phase-locked phenotype.

Citations

Citations to this article as recorded by  
  • Encapsulated Ferritin-like Proteins: A Structural Perspective
    Elif Eren, Norman R. Watts, Felipe Montecinos, Paul T. Wingfield
    Biomolecules.2024; 14(6): 624.     CrossRef
  • A widespread bacterial protein compartment sequesters and stores elemental sulfur
    Robert Benisch, Michael P. Andreas, Tobias W. Giessen
    Science Advances.2024;[Epub]     CrossRef
  • Structure and heterogeneity of a highly cargo-loaded encapsulin shell
    Seokmu Kwon, Michael P. Andreas, Tobias W. Giessen
    Journal of Structural Biology.2023; 215(4): 108022.     CrossRef
  • Bacterial Nanocompartments: Structures, Functions, and Applications
    Harry Benjamin McDowell, Egbert Hoiczyk, Michael Y. Galperin
    Journal of Bacteriology.2022;[Epub]     CrossRef
  • Condensation and Protection of DNA by the Myxococcus xanthus Encapsulin: A Novel Function
    Ana V. Almeida, Ana J. Carvalho, Tomás Calmeiro, Nykola C. Jones, Søren V. Hoffmann, Elvira Fortunato, Alice S. Pereira, Pedro Tavares
    International Journal of Molecular Sciences.2022; 23(14): 7829.     CrossRef
  • Encapsulins
    Tobias W. Giessen
    Annual Review of Biochemistry.2022; 91(1): 353.     CrossRef
  • Advances in encapsulin nanocompartment biology and engineering
    Jesse A. Jones, Tobias W. Giessen
    Biotechnology and Bioengineering.2021; 118(1): 491.     CrossRef
  • Encapsulin nanocages: Protein encapsulation and iron sequestration
    Ana V. Almeida, Ana J. Carvalho, Alice S. Pereira
    Coordination Chemistry Reviews.2021; 448: 214188.     CrossRef
  • Discovery and characterization of a novel family of prokaryotic nanocompartments involved in sulfur metabolism
    Robert J Nichols, Benjamin LaFrance, Naiya R Phillips, Devon R Radford, Luke M Oltrogge, Luis E Valentin-Alvarado, Amanda J Bischoff, Eva Nogales, David F Savage
    eLife.2021;[Epub]     CrossRef
  • Nanotechnological Applications Based on Bacterial Encapsulins
    Javier M. Rodríguez, Carolina Allende-Ballestero, Jeroen J. L. M. Cornelissen, José R. Castón
    Nanomaterials.2021; 11(6): 1467.     CrossRef

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