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Instruments / Technical Area	Publication Details	Published
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
B21-High Throughput SAXS I02-Macromolecular Crystallography I04-1-Macromolecular Crystallography (fixed wavelength)	Structural basis of host Autophagy-related protein 8 (ATG8) binding by the Irish potato famine pathogen effector protein PexRD54 Abbas Maqbool , Richard Hughes , Yasin F Dagdas , Nicholas Tregidgo , Erin Zess , Khaoula Belhaj , Adam Round , Tolga O Bozkurt , Sophien Kamoun , Mark Banfield Journal Of Biological Chemistry DOI: 10.1074/jbc.M116.744995 Diamond Proposal Number(s): [7641] Show Abstract ▼ Abstract: Filamentous plant pathogens deliver effector proteins to host cells to promote infection. The Phytophthora infestans RXLR-type effector PexRD54 binds potato ATG8 via its ATG8-family interacting motif (AIM) and perturbs host selective autophagy. However, the structural basis of this interaction remains unknown. Here we define the crystal structure of PexRD54, which comprises a modular architecture including five tandem repeat domains, with the AIM sequence presented at the disordered C-terminus. To determine the interface between PexRD54 and ATG8, we solved the crystal structure of potato ATG8CL in complex with a peptide comprising the effector’s AIM sequence, and established a model of the full-length PexRD54/ATG8CL complex using small angle X-ray scattering. Structure-informed deletion of the PexRD54 tandem domains reveals retention of ATG8CL binding in vitro and in planta. This study offers new insights into structure/function relationships of oomycete RXLR effectors and how these proteins engage with host cell targets to promote disease.	Jul 2016
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
I02-Macromolecular Crystallography I04-Macromolecular Crystallography	Oomycetes, effectors, and all that jazz Tolga O. Bozkurt , Sebastian Schornack , Mark J. Banfield , Sophien Kamoun Current Opinion In Plant Biology 15 (4), 483 - 492 DOI: 10.1016/j.pbi.2012.03.008 Diamond Proposal Number(s): [7641] Show Abstract ▼ Abstract: Plant pathogenic oomycetes secrete a diverse repertoire of effector proteins that modulate host innate immunity and enable parasitic infection. Understanding how effectors evolve, translocate and traffic inside host cells, and perturb host processes are major themes in the study of oomycete–plant interactions. The last year has seen important progress in the study of oomycete effectors with, notably, the elucidation of the 3D structures of five RXLR effectors, and novel insights into how cytoplasmic effectors subvert host cells. In this review, we discuss these and other recent advances and highlight the most important open questions in oomycete effector biology.	Aug 2012
I02-Macromolecular Crystallography I04-Macromolecular Crystallography	Sequence Divergent RXLR Effectors Share a Structural Fold Conserved across Plant Pathogenic Oomycete Species Joe Win , Ksenia V. Krasileva , Sophien Kamoun , Ken Shirasu , Brian J. Staskawicz , Mark J. Banfield PLoS Pathogens 8 (1) DOI: 10.1371/journal.ppat.1002400 PMID: 22253591 Diamond Proposal Number(s): [7641] Open Access Show Abstract ▼ Abstract: The availability of genome sequences for some of the most devastating eukaryotic plant pathogens has led a revolution in our understanding of how these parasites cause disease, and how their hosts respond to invasion. One of the most significant discoveries from the genome sequences of plant pathogenic oomycetes is the plethora of putative translocated effector proteins these organisms encode. Many effector genes display signatures of rapid evolution and tend to reside in dynamic regions of the pathogen genomes. Once inside the host, effector proteins modulate cellular processes, mainly suppressing plant immunity. Effectors can also be recognized directly or indirectly by the plant immune system through the action of disease resistance proteins	Jan 2012
I02-Macromolecular Crystallography I04-Macromolecular Crystallography	Structures of Phytophthora RXLR effector proteins: a conserved but adaptable fold underpins functional diversity Laurence Boutemy , Stuart R. F. King , Joe Win , Richard K. Hughes , Thomas A. Clarke , Tharin Blumenschein , Sophien Kamoun , Mark J. Banfield Journal Of Biological Chemistry DOI: 10.1074/jbc.M111.262303 PMID: 21813644 Show Abstract ▼ Abstract: Phytopathogens deliver effector proteins inside host plant cells to promote infection. These proteins can also be sensed by the plant immune system, leading to restriction of pathogen growth. Effector genes can display signatures of positive selection and rapid evolution, presumably a consequence of their co-evolutionary arms race with plants. The molecular mechanisms underlying how effectors evolve to gain new virulence functions and/or evade the plant immune system are poorly understood. Here, we report the crystal structures of the effector domains from two oomycete RXLR proteins, Phytophthora capsici AVR3a11 and Phytophthora infestans PexRD2. Despite sharing < 20% sequence identity in their effector domains they display a conserved core α-helical fold. Bioinformatic analyses suggest the core fold occurs in ~44% of annotated Phytophthora RXLR effectors, both as a single domain and in tandem repeats of up to 11 units. Functionally important and polymorphic residues map to the surface of the structures and PexRD2, but not AVR3a11, oligomerizes in planta. We conclude that the core α-helical fold enables functional adaptation of these fast-evolving effectors through (i) insertion/deletions in loop regions between α-helices, (ii) extensions to the N- and C-termini, (iii) amino acid replacements in surface residues, (iv) tandem domain duplications and (v) oligomerization. We hypothesize that the molecular stability provided by this core fold, combined with considerable potential for plasticity, underlies the evolution of effectors that maintain their virulence activities while evading recognition by the plant immune system.	Aug 2011

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