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Instruments / Technical Area	Publication Details	Published	Actions
I04-Macromolecular Crystallography	Structural basis of pathogen recognition by an integrated HMA domain in a plant NLR immune receptor Abbas Maqbool , H Saitoh , M Franceschetti , Cem Stevenson , A Uemura , H Kanzaki , S Kamoun , R Terauchi , M. J Banfield Elife 4 DOI: 10.7554/eLife.08709 PMID: 26304198 Diamond Proposal Number(s): [7641, 9475] Open Access Show Abstract ▼ 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.	Aug 2015
I03-Macromolecular Crystallography I04-Macromolecular Crystallography	Polymorphic residues in rice NLRs expand binding and response to effectors of the blast pathogen Juan Carlos De La Concepcion , Marina Franceschetti , Abbas Maqbool , Hiromasa Saitoh , Ryohei Terauchi , Sophien Kamoun , Mark J. Banfield Nature Plants 354 DOI: 10.1038/s41477-018-0194-x Diamond Proposal Number(s): [9475, 13467] Show Abstract ▼ 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.	Jul 2018

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