Poster
Kira Gysel
Assistant Professor
Department of Molecular Biology and Genetics, Aarhus University
Aarhus, Midtjylland, Denmark
Simon B. Hansen
Department of Molecular Biology and Genetics, Aarhus University
Zürich, Zurich, Switzerland
Henriette Rübsam
Department of Molecular Biology and Genetics, Aarhus University
Aarhus C, Midtjylland, Denmark
Husam Alsarraf
Department of Molecular Biology and Genetics, Aarhus University
Aarhus C, Midtjylland, Denmark
Eva Madland
Department of Molecular Biology and Genetics, Aarhus University
Aarhus C, Midtjylland, Denmark
Caroline Baadegaard
Department of Molecular Biology and Genetics, Aarhus University
Aarhus C, Midtjylland, Denmark
Emil Poulsen
Department of Molecular Biology and Genetics, Aarhus University
Aarhus C, Midtjylland, Denmark
Maria Vinther
Department of Molecular Biology and Genetics, Aarhus University
Aarhus, Midtjylland, Denmark
Sébastien Fort
Univ. Grenoble Alpes, CNRS, CERMAV
Grenoble, Rhone-Alpes, France
Jens Stougaard
Department of Molecular Biology and Genetics, Aarhus University
Aarhus, Midtjylland, Denmark
Kasper Andersen
Department of Molecular Biology and Genetics, Aarhus University
Aarhus, Midtjylland, Denmark
Plants rely on innate pattern recognition receptors to detect microbe-associated molecular patterns (MAMPs) and activate immunity. This study elucidates the molecular mechanisms for the specific recognition of long-chain chitin oligomers (e.g. chitooctaose), a major MAMP found in the fungal cell wall. In the legumes Lotus japonicus and Medicago truncatula, perception of these immunogenic long-chain chitin oligomers is facilitated by the LysM receptor kinases LYS13/CERK6 and LYR4/CERK1, respectively. We combine structural biology, quantitative ligand binding assays, biochemistry, and functional data to provide a thorough understanding of how LYS13- and CERK-type receptors function in concert to induce immune signaling in plants. In addition, we use specific nanobodies to directly modulate plant immunity, probing receptor binding sites and ligand-induced complex formation. Key results include the identification of detailed mechanisms for size-selective, high-affinity long chitin oligomer binding by LYS13-type receptors, as well as the characterization of the CERK-type receptors as low-affinity co-receptors. We present a mechanistic model for LysM receptor kinase assembly into a signaling-competent receptor complex upon chitin perception, where the high-affinity pseudokinase LYS13 recruits the low-affinity active kinase CERK6 via a ligand-induced mechanism.