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Structural basis of pathogen recognition by an integrated HMA domain in a plant NLR immune receptor

DOI: 10.7554/eLife.08709 DOI Help
PMID: 26304198 PMID Help

Authors: Abbas Maqbool (John Innes Centre) , H Saitoh (Iwate Biotechnology Research Center, Japan) , M Franceschetti (John Innes Centre) , Cem Stevenson (John Innes Centre) , A Uemura (Iwate Biotechnology Research Center, Japan) , H Kanzaki (Iwate Biotechnology Research Center, Japan) , S Kamoun (The Sainsbury Laboratory) , R Terauchi (Iwate Biotechnology Research Center, Japan) , M. J Banfield (John Innes Centre)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Elife , VOL 4

State: Published (Approved)
Published: August 2015
Diamond Proposal Number(s): 7641 , 9475

Open Access Open Access

Abstract: Plants have evolved intracellular immune receptors to detect pathogen proteins known as effectors. How these immune receptors detect effectors remains poorly understood. Here we describe the structural basis for direct recognition of AVR-Pik, an effector from the rice blast pathogen, by the rice intracellular NLR immune receptor Pik. AVR-PikD binds a dimer of the Pikp-1 HMA integrated domain with nanomolar affinity. The crystal structure of the Pikp-HMA/AVR-PikD complex enabled design of mutations to alter protein interaction in yeast and in vitro, and perturb effector-mediated response both in a rice cultivar containing Pikp and upon expression of AVR-PikD and Pikp in the model plant Nicotiana benthamiana. These data reveal the molecular details of a recognition event, mediated by a novel integrated domain in an NLR, which initiates a plant immune response and resistance to rice blast disease. Such studies underpin novel opportunities for engineering disease resistance to plant pathogens in staple food crops.

Journal Keywords: Rice; Rice Blast Disease; Plant Disease Resistance; Effector Protein; Integrated Sensor Domain

Subject Areas: Biology and Bio-materials


Instruments: I04-Macromolecular Crystallography