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Polymorphic residues in rice NLRs expand binding and response to effectors of the blast pathogen

DOI: 10.1038/s41477-018-0194-x DOI Help

Authors: Juan Carlos De La Concepcion (John Innes Centre) , Marina Franceschetti (John Innes Centre) , Abbas Maqbool (John Innes Centre) , Hiromasa Saitoh (Tokyo University of Agriculture) , Ryohei Terauchi (Iwate Biotechnology Research Center; Kyoto University) , Sophien Kamoun (The Sainsbury Laboratory) , Mark J. Banfield (John Innes Centre)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Plants , VOL 354

State: Published (Approved)
Published: July 2018
Diamond Proposal Number(s): 9475 , 13467

Abstract: Accelerated adaptive evolution is a hallmark of plant–pathogen interactions. Plant intracellular immune receptors (NLRs) often occur as allelic series with differential pathogen specificities. The determinants of this specificity remain largely unknown. Here, we unravelled the biophysical and structural basis of expanded specificity in the allelic rice NLR Pik, which responds to the effector AVR-Pik from the rice blast pathogen Magnaporthe oryzae. Rice plants expressing the Pikm allele resist infection by blast strains expressing any of three AVR-Pik effector variants, whereas those expressing Pikp only respond to one. Unlike Pikp, the integrated heavy metal-associated (HMA) domain of Pikm binds with high affinity to each of the three recognized effector variants, and variation at binding interfaces between effectors and Pikp-HMA or Pikm-HMA domains encodes specificity. By understanding how co-evolution has shaped the response profile of an allelic NLR, we highlight how natural selection drove the emergence of new receptor specificities. This work has implications for the engineering of NLRs with improved utility in agriculture.

Journal Keywords: Effectors in plant pathology; Structure determination

Subject Areas: Biology and Bio-materials


Instruments: I03-Macromolecular Crystallography , I04-Macromolecular Crystallography