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<p>Plant peptide hormones play essential roles in various physiological processes, including activating defence responses to biotic stress. Membrane-localized pattern recognition receptors (PRRs) typically detect peptide hormones to initiate signalling pathways. Through comprehensive peptide–receptor matching, we identified 63 peptide–receptor pairs in soybeans. Among these, the immunomodulatory phytocytokines GmPEP914 and GmPEP890 trigger robust immune responses that suppress a broad spectrum of pathogen infections, mediated by their identified receptors GmPEP914 and GmPEP890 RECEPTOR1 (GmP98R1) and GmP98R2. Biochemical assays combined with AI-based structural modelling demonstrated that both peptides directly bind GmP98Rs with nanomolar affinity, driven primarily by interactions between the receptors and the C-terminal residue of the peptides. The PEP914-P98R module is conserved across Fabales and Cucurbitales, underscoring its evolutionary importance. Collectively, our study establishes a scalable pipeline for systematic peptide–receptor discovery and elucidates the pivotal role of the PEP914-P98R module in soybean disease resistance.</p>

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Large-scale pairing identifies a soybean phytocytokine-receptor module conferring disease resistance

  • 期刊论文

  • 发表日期：

    2025年8月19日

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  • Liping Yu,
  • Yiwen Gao,
  • Qiujiao Yang,
  • Jing Liu,
  • Tengfei Liu,
  • Weiping Mo,
  • Hangqin Liu,
  • Zhixi Tian,
  • Lei Li

摘要

Plant peptide hormones play essential roles in various physiological processes, including activating defence responses to biotic stress. Membrane-localized pattern recognition receptors (PRRs) typically detect peptide hormones to initiate signalling pathways. Through comprehensive peptide–receptor matching, we identified 63 peptide–receptor pairs in soybeans. Among these, the immunomodulatory phytocytokines GmPEP914 and GmPEP890 trigger robust immune responses that suppress a broad spectrum of pathogen infections, mediated by their identified receptors GmPEP914 and GmPEP890 RECEPTOR1 (GmP98R1) and GmP98R2. Biochemical assays combined with AI-based structural modelling demonstrated that both peptides directly bind GmP98Rs with nanomolar affinity, driven primarily by interactions between the receptors and the C-terminal residue of the peptides. The PEP914-P98R module is conserved across Fabales and Cucurbitales, underscoring its evolutionary importance. Collectively, our study establishes a scalable pipeline for systematic peptide–receptor discovery and elucidates the pivotal role of the PEP914-P98R module in soybean disease resistance.