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Plant Cell. 2017 Jan;29(1):156-168. doi: 10.1105/tpc.16.00435. Epub 2017 Jan 13.

Recognition of the Magnaporthe oryzae Effector AVR-Pia by the Decoy Domain of the Rice NLR Immune Receptor RGA5.

Author information

1
INRA, BGPI, Biology and Genetics of Plant-Pathogen Interactions, Campus International de Baillarguet, 34398 Montpellier, France.
2
CNRS UMR 5048, INSERM U1054, Centre de Biochimie Structurale, Université Montpellier, 34090 Montpellier, France.
3
CSIRO Agriculture Flagship, Canberra ACT 2601, Australia.
4
INRA, BGPI, Biology and Genetics of Plant-Pathogen Interactions, Campus International de Baillarguet, 34398 Montpellier, France thomas.kroj@inra.fr.

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 the Magnaporthe oryzae effector 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.

PMID:
28087830
PMCID:
PMC5304345
DOI:
10.1105/tpc.16.00435
[Indexed for MEDLINE]
Free PMC Article

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