Arabidopsis immune responses triggered by cellulose and mixed-linked glucan oligosaccharides require a group of Leucine-Rich Repeat-Malectin Receptor Kinases.


Journal article


Marina Martín-Dacal, Patricia Fernández-Calvo, P. Jiménez-Sandoval, G. López, M. Garrido‐Arandia, Diego Rebaque, Irene del Hierro, Diego José Berlanga, M. Torres, Varun Kumar, Hugo Mélida, L. Pacios, J. Santiago, A. Molina
The Plant Journal, 2022

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APA   Click to copy
Martín-Dacal, M., Fernández-Calvo, P., Jiménez-Sandoval, P., López, G., Garrido‐Arandia, M., Rebaque, D., … Molina, A. (2022). Arabidopsis immune responses triggered by cellulose and mixed-linked glucan oligosaccharides require a group of Leucine-Rich Repeat-Malectin Receptor Kinases. The Plant Journal.


Chicago/Turabian   Click to copy
Martín-Dacal, Marina, Patricia Fernández-Calvo, P. Jiménez-Sandoval, G. López, M. Garrido‐Arandia, Diego Rebaque, Irene del Hierro, et al. “Arabidopsis Immune Responses Triggered by Cellulose and Mixed-Linked Glucan Oligosaccharides Require a Group of Leucine-Rich Repeat-Malectin Receptor Kinases.” The Plant Journal (2022).


MLA   Click to copy
Martín-Dacal, Marina, et al. “Arabidopsis Immune Responses Triggered by Cellulose and Mixed-Linked Glucan Oligosaccharides Require a Group of Leucine-Rich Repeat-Malectin Receptor Kinases.” The Plant Journal, 2022.


BibTeX   Click to copy

@article{marina2022a,
  title = {Arabidopsis immune responses triggered by cellulose and mixed-linked glucan oligosaccharides require a group of Leucine-Rich Repeat-Malectin Receptor Kinases.},
  year = {2022},
  journal = {The Plant Journal},
  author = {Martín-Dacal, Marina and Fernández-Calvo, Patricia and Jiménez-Sandoval, P. and López, G. and Garrido‐Arandia, M. and Rebaque, Diego and del Hierro, Irene and Berlanga, Diego José and Torres, M. and Kumar, Varun and Mélida, Hugo and Pacios, L. and Santiago, J. and Molina, A.}
}

Abstract

The plant immune system perceives a diversity of carbohydrate ligands from plant and microbial cell walls through the extracellular ectodomains (ECDs) of Pattern Recognition Receptors (PRRs), which activate Pattern-Triggered Immunity (PTI). Among these ligands are oligosaccharides derived from mixed-linked β-1,3/β-1,4-glucans (MLGs, e.g., β-1,4-D-(Glc)2 -β-1,3-D-Glc, MLG43) and cellulose (e.g., β-1,4-D-(Glc)3 , CEL3). The mechanisms of carbohydrates perception by plants are poorly characterised, except for fungal chitin oligosaccharides (e.g., β-1,4-D(GlcNAc)6 , CHI6) that involves several Receptor Kinase proteins (RK) with LysM-ECDs. Here, we describe the isolation and characterisation of Arabidopsis thaliana mutants impaired in glycan perception (igp) that are defective in PTI activation mediated by MLG43 and CEL3, but not by CHI6. igp1-igp4 are altered in three RKs [AT1G56145 (IGP1), AT1G56130 (IGP2/IGP3), and AT1G56140 (IGP4)] with Leucine-Rich-Repeat (LRR) and Malectin (MAL) domains in their ECDs. igp1 and igp2/3 harbour point mutations (E906K and G773E, respectively) in their kinase domains whereas igp4 is a T-DNA insertional, loss of function mutant. Notably, Isothermal Titration Calorimetry (ITC) assays with purified ECD-RKs of IGP1 and IGP3 showed that IGP1 binds with high-affinity CEL3 (Kd = 1.19 ± 0.03 μM) and cellopentaose (Kd = 1.40 ± 0.01 μM), but not MLG43, supporting its function as a plant PRR for cellulose oligosaccharides. Our data suggest that these LRR-MAL RKs are components of a novel recognition mechanism for both cellulose and MLG-derived oligosaccharides perception and downstream PTI activation in Arabidopsis.