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

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


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites / genetics
  • Disease Resistance / genetics
  • Fungal Proteins / chemistry
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism*
  • Host-Pathogen Interactions
  • Magnaporthe / genetics
  • Magnaporthe / metabolism*
  • Magnaporthe / physiology
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Mutation
  • Oryza / genetics
  • Oryza / metabolism*
  • Oryza / microbiology
  • Plant Diseases / genetics
  • Plant Diseases / microbiology
  • Plant Immunity / genetics
  • Plant Leaves / genetics
  • Plant Leaves / metabolism
  • Plant Leaves / microbiology
  • Plant Proteins / chemistry
  • Plant Proteins / genetics
  • Plant Proteins / metabolism*
  • Protein Binding
  • Protein Domains
  • Receptors, Immunologic / chemistry
  • Receptors, Immunologic / genetics
  • Receptors, Immunologic / metabolism*


  • Fungal Proteins
  • Plant Proteins
  • Receptors, Immunologic