title: Recognition of theMagnaporthe oryzaeEffector AVR-Pia by the Decoy Domain of the Rice NLR Immune Receptor RGA5.
abstract: Nucleotide binding domain and leucine-rich repeat proteins (NLRs) are important receptors in plant immunity that allow recognition of pathogen effectors. The rice (Oryza sativa) NLR RGA5 recognizes theMagnaporthe oryzaeeffector AVR-Pia through direct interaction. Here, we gained detailed insights into the molecular and structural bases of AVR-Pia-RGA5 interaction and the role of the RATX1 decoy domain of RGA5. NMR titration combined with in vitro and in vivo protein-protein interaction analyses identified the AVR-Pia interaction surface that binds to the RATX1 domain. Structure-informed AVR-Pia mutants showed that, although AVR-Pia associates with additional sites in RGA5, binding to the RATX1 domain is necessary for pathogen recognition but can be of moderate affinity. Therefore, RGA5-mediated resistance is highly resilient to mutations in the effector. We propose a model that explains such robust effector recognition as a consequence, and an advantage, of the combination of integrated decoy domains with additional independent effector-NLR interactions.
authors.affiliation: INRA, BGPI, Biology and Genetics of Plant-Pathogen Interactions, Campus International de Baillarguet, 34398 Montpellier, France.
authors.forename: Diana
authors.initials: D
authors.lastname: Ortiz
authors.affiliation: CNRS UMR 5048, INSERM U1054, Centre de Biochimie Structurale, Université Montpellier, 34090 Montpellier, France.
authors.forename: Karine
authors.initials: K
authors.lastname: de Guillen
authors.affiliation: INRA, BGPI, Biology and Genetics of Plant-Pathogen Interactions, Campus International de Baillarguet, 34398 Montpellier, France.|CSIRO Agriculture Flagship, Canberra ACT 2601, Australia.
authors.forename: Stella
authors.initials: S
authors.lastname: Cesari
authors.affiliation: INRA, BGPI, Biology and Genetics of Plant-Pathogen Interactions, Campus International de Baillarguet, 34398 Montpellier, France.
authors.forename: Véronique
authors.initials: V
authors.lastname: Chalvon
authors.affiliation: CNRS UMR 5048, INSERM U1054, Centre de Biochimie Structurale, Université Montpellier, 34090 Montpellier, France.
authors.forename: Jérome
authors.identifier: 0000-0002-9778-0327
authors.initials: J
authors.lastname: Gracy
authors.affiliation: CNRS UMR 5048, INSERM U1054, Centre de Biochimie Structurale, Université Montpellier, 34090 Montpellier, France.
authors.forename: André
authors.identifier: 0000-0001-9702-4612
authors.initials: A
authors.lastname: Padilla
authors.affiliation: INRA, BGPI, Biology and Genetics of Plant-Pathogen Interactions, Campus International de Baillarguet, 34398 Montpellier, France thomas.kroj@inra.fr.
authors.forename: Thomas
authors.identifier: 0000-0002-3752-1788
authors.initials: T
authors.lastname: Kroj
mesh_terms: D001665:Binding Sites / Q000235:genetics; D060467:Disease Resistance / Q000235:genetics; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D054884:Host-Pathogen Interactions; D020082:Magnaporthe / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D009154:Mutation; D012275:Oryza / Q000235:genetics / Q000378:metabolism* / Q000382:microbiology; D010935:Plant Diseases / Q000235:genetics / Q000382:microbiology; D057865:Plant Immunity / Q000235:genetics; D018515:Plant Leaves / Q000235:genetics / Q000378:metabolism / Q000382:microbiology; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D000072417:Protein Domains; D011971:Receptors, Immunologic / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D005656:Fungal Proteins; D010940:Plant Proteins; D011971:Receptors, Immunologic