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Poster

Session: Session 1 Presenting Authors at Posters (Odds)

P-437 - Β-sheet stabilization of the island domain underlies ligand-induced LRR-RLP activation of plant immune signaling

Monday, July 14, 2025
13:30 - 15:15  
Location: Confex Hall 3
Structure Informed Synthetic Biology: From Design to Function

    Presenting Author(s)

  • SS

    Simon Snoeck

    University of Zurich
    Zurich, SWITZERLAND

    • Author(s)

  • LZ

    Lisha Zhang

    Dr
    University of Tübingen
    Tuebingen, Baden-Wurttemberg, Germany

  • VS

    Valentin Studer

    ETH Zurich
    Zurich, Zurich, Switzerland

  • GK

    Gijeong Kim

    Institute of Plant and Microbial Biology, University of Zurich
    Zurich, Zurich, Switzerland

  • F

    Álvaro D. Fernández-Fernández

    Institute of Plant and Microbial Biology, University of Zurich
    Zurich, Zurich, Switzerland

  • TN

    Thorsten Nuernberger

    University of Tü​bingen
    Tuebingen, Baden-Wurttemberg, Germany

  • CZ

    Cyril Zipfel

    Institute of Plant and Microbial Biology, University of Zurich / The Sainsbury Laboratory
    Zurich, Zurich, Switzerland

Leucine-rich repeat (LRR) receptor kinases (RKs) and receptor proteins (RPs) are important classes of plant pattern recognition receptors (PRRs) activating pattern-triggered immunity. We recently published an AI-based alternative to classical structure-based approaches for resolving ligand-LRR-RK-binding mechanisms (Snoeck et al., 2024). However, the majority of LRR-RKs have a relatively simpler extracellular architecture than LRR-RPs which typically embed one or more loopout regions in their extracellular domains that are crucial for functionality. We here further developed our AI-based approach to reveal a novel ligand-binding mechanism shared by RLP23 and RLP42 – the PRRs for necrosis and ethylene-inducing peptide 1-like proteins (NLPs) and fungal endopolygalacturonases (PGs), respectively – through anti B-sheet interaction with the island domain (ID) loopout. Additionally, we investigated the larger and more complex binding interfaces of RLP32 and RE02 – the PRRs for proteobacterial translation initiation factor 1 (IF1) and fungal/oomycete small cysteine-rich protein (SCP), respectively. 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 of this important class of PRRs, which open avenues for a molecular understanding of the co-evolution between plants and their pathogens, as well as the engineering of plant immune receptors for crop disease resistance.