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<p>Leucine-rich repeat (LRR) receptor kinases (RKs) and receptor proteins (RPs) are important classes of plant pattern recognition receptors (PRRs) activating pattern-triggered immunity. While both classical and AI-based structural approaches have recently provided crucial insights into ligand-LRR-RK binding mechanisms, our understanding of ligand perception by LRR-RPs remains limited. Here, we employed an AI-based approach to reveal a ligand-binding mechanism shared by the Arabidopsis LRR-RPs RLP23 and RLP42 – the PRRs for the short peptide ligands nlp20 and pg13, derived from NECROSIS- AND ETHYLENE-INDUCING PEPTIDE 1-like proteins (NLPs) and fungal endopolygalacturonases (PGs), respectively. Additionally, we investigated the larger and more complex binding interface of RLP32 – the PRR for proteobacterial TRANSLATION INITIATION FACTOR 1 (IF1), a folded protein ligand that requires its tertiary structure for recognition. Finally, we describe a mechanistic role of the ID for co-receptor recruitment conserved across LRR-RPs. Together, our results shed light on the ligand-binding mechanisms and receptor complex formation of LRR-RPs, opening avenues for their engineering for crop disease resistance.</p>

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β-sheet stabilization of the island domain underlies ligand-induced LRR-RP activation of plant immune signaling

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年12月8日

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  • Simon Snoeck,
  • Lisha Zhang,
  • Valentin Studer,
  • Gijeong Kim,
  • Álvaro D. Fernández-Fernández,
  • Thorsten Nürnberger,
  • Cyril Zipfel

摘要

Leucine-rich repeat (LRR) receptor kinases (RKs) and receptor proteins (RPs) are important classes of plant pattern recognition receptors (PRRs) activating pattern-triggered immunity. While both classical and AI-based structural approaches have recently provided crucial insights into ligand-LRR-RK binding mechanisms, our understanding of ligand perception by LRR-RPs remains limited. Here, we employed an AI-based approach to reveal a ligand-binding mechanism shared by the Arabidopsis LRR-RPs RLP23 and RLP42 – the PRRs for the short peptide ligands nlp20 and pg13, derived from NECROSIS- AND ETHYLENE-INDUCING PEPTIDE 1-like proteins (NLPs) and fungal endopolygalacturonases (PGs), respectively. Additionally, we investigated the larger and more complex binding interface of RLP32 – the PRR for proteobacterial TRANSLATION INITIATION FACTOR 1 (IF1), a folded protein ligand that requires its tertiary structure for recognition. Finally, we describe a mechanistic role of the ID for co-receptor recruitment conserved across LRR-RPs. Together, our results shed light on the ligand-binding mechanisms and receptor complex formation of LRR-RPs, opening avenues for their engineering for crop disease resistance.