title: Host protein BSL1 associates with Phytophthora infestans RXLR effector AVR2 and the Solanum demissum Immune receptor R2 to mediate disease resistance.
abstract: Plant pathogens secrete effector proteins to modulate plant immunity and promote host colonization. Plant nucleotide binding leucine-rich repeat (NB-LRR) immunoreceptors recognize specific pathogen effectors directly or indirectly. Little is known about how NB-LRR proteins recognize effectors of filamentous plant pathogens, such as Phytophthora infestans. AVR2 belongs to a family of 13 sequence-divergent P. infestans RXLR effectors that are differentially recognized by members of the R2 NB-LRR family in Solanum demissum. We report that the putative plant phosphatase BSU-LIKE PROTEIN1 (BSL1) is required for R2-mediated perception of AVR2 and resistance to P. infestans. AVR2 associates with BSL1 and mediates the interaction of BSL1 with R2 in planta, possibly through the formation of a ternary complex. Strains of P. infestans that are virulent on R2 potatoes express an unrecognized form, Avr2-like (referred to as A2l). A2L can still interact with BSL1 but does not promote the association of BSL1 with R2. Our findings show that recognition of the P. infestans AVR2 effector by the NB-LRR protein R2 requires the putative phosphatase BSL1. This reveals that, similar to effectors of phytopathogenic bacteria, recognition of filamentous pathogen effectors can be mediated via a host protein that interacts with both the effector and the NB-LRR immunoreceptor.
authors.affiliation: The Sainsbury Laboratory, Norwich Research Park, Norwich NR4 7UH, United Kingdom.
authors.forename: Diane G O
authors.initials: DG
authors.lastname: Saunders
authors.forename: Susan
authors.initials: S
authors.lastname: Breen
authors.forename: Joe
authors.initials: J
authors.lastname: Win
authors.forename: Sebastian
authors.initials: S
authors.lastname: Schornack
authors.forename: Ingo
authors.initials: I
authors.lastname: Hein
authors.forename: Tolga O
authors.initials: TO
authors.lastname: Bozkurt
authors.forename: Nicolas
authors.initials: N
authors.lastname: Champouret
authors.forename: Vivianne G A A
authors.initials: VG
authors.lastname: Vleeshouwers
authors.forename: Paul R J
authors.initials: PR
authors.lastname: Birch
authors.forename: Eleanor M
authors.initials: EM
authors.lastname: Gilroy
authors.forename: Sophien
authors.initials: S
authors.lastname: Kamoun
mesh_terms: D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000378:metabolism; D060467:Disease Resistance; D054884:Host-Pathogen Interactions; D047468:Immunoprecipitation; D000090263:Leucine-Rich Repeat Proteins; D008969:Molecular Sequence Data; D010744:Phosphoric Monoester Hydrolases / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D055750:Phytophthora infestans / Q000276:immunology / Q000472:pathogenicity*; D010935:Plant Diseases / Q000276:immunology / Q000382:microbiology; D057865:Plant Immunity; D010940:Plant Proteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D010957:Plasmids / Q000235:genetics / Q000378:metabolism; D025941:Protein Interaction Mapping; D055550:Protein Stability; D011506:Proteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D011956:Receptors, Cell Surface / Q000276:immunology / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D032322:Solanum / Q000201:enzymology / Q000276:immunology / Q000382:microbiology*; D013379:Substrate Specificity; D020798:Two-Hybrid System Techniques
chemical_list: D000090263:Leucine-Rich Repeat Proteins; D010940:Plant Proteins; D011506:Proteins; D011956:Receptors, Cell Surface; D011993:Recombinant Fusion Proteins; D010744:Phosphoric Monoester Hydrolases