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A plant cell death-inducing protein from litchi interacts with Peronophythora litchii pectate lyase and enhances plant resistance

Author

Listed:
  • Wen Li

    (South China Agricultural University)

  • Peng Li

    (South China Agricultural University)

  • Yizhen Deng

    (South China Agricultural University)

  • Junjian Situ

    (South China Agricultural University)

  • Zhuoyuan He

    (South China Agricultural University)

  • Wenzhe Zhou

    (South China Agricultural University)

  • Minhui Li

    (South China Agricultural University)

  • Pinggen Xi

    (South China Agricultural University)

  • Xiangxiu Liang

    (South China Agricultural University)

  • Guanghui Kong

    (South China Agricultural University)

  • Zide Jiang

    (South China Agricultural University)

Abstract

Cell wall degrading enzymes, including pectate lyases (PeLs), released by plant pathogens, break down protective barriers and/or activate host immunity. The direct interactions between PeLs and plant immune-related proteins remain unclear. We identify two PeLs, PlPeL1 and PlPeL1-like, critical for full virulence of Peronophythora litchii on litchi (Litchi chinensis). These proteins enhance plant susceptibility to oomycete pathogens in a PeL enzymatic activity-dependent manner. However, LcPIP1, a plant immune regulator secreted by litchi, binds to PlPeL1/PlPeL1-like, and attenuates PlPeL1/PlPeL1-like induced plant susceptibility to Phytophthora capsici. LcPIP1 also induces cell death and various immune responses in Nicotiana benthamiana. Conserved in plants, LcPIP1 homologs bear a conserved “VDMASG” motif and exhibit immunity-inducing activity. Furthermore, SERK3 interacts with LcPIP1 and is required for LcPIP1-induced cell death. NbPIP1 participates in immune responses triggered by the PAMP protein INF1. In summary, our study reveals the dual roles of PlPeL1/PlPeL1-like in plant-pathogen interactions: enhancing pathogen virulence through PeL enzymatic activity while also being targeted by LcPIP1, thus enhancing plant immunity.

Suggested Citation

  • Wen Li & Peng Li & Yizhen Deng & Junjian Situ & Zhuoyuan He & Wenzhe Zhou & Minhui Li & Pinggen Xi & Xiangxiu Liang & Guanghui Kong & Zide Jiang, 2024. "A plant cell death-inducing protein from litchi interacts with Peronophythora litchii pectate lyase and enhances plant resistance," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-023-44356-y
    DOI: 10.1038/s41467-023-44356-y
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    References listed on IDEAS

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    1. Wei Wei & Liangsheng Xu & Hao Peng & Wenjun Zhu & Kiwamu Tanaka & Jiasen Cheng & Karen A. Sanguinet & George Vandemark & Weidong Chen, 2022. "A fungal extracellular effector inactivates plant polygalacturonase-inhibiting protein," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    2. Zheng Qing Fu & Shunping Yan & Abdelaty Saleh & Wei Wang & James Ruble & Nodoka Oka & Rajinikanth Mohan & Steven H. Spoel & Yasuomi Tada & Ning Zheng & Xinnian Dong, 2012. "NPR3 and NPR4 are receptors for the immune signal salicylic acid in plants," Nature, Nature, vol. 486(7402), pages 228-232, June.
    3. Yue Sun & Yan Wang & Xiaoxiao Zhang & Zhaodan Chen & Yeqiang Xia & Lei Wang & Yujing Sun & Mingmei Zhang & Yu Xiao & Zhifu Han & Yuanchao Wang & Jijie Chai, 2022. "Plant receptor-like protein activation by a microbial glycoside hydrolase," Nature, Nature, vol. 610(7931), pages 335-342, October.
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