Host Protein BSL1 Associates with Phytophthora infestans RXLR Effector AVR2 and the Solanum demissum Immune Receptor R2 to Mediate Disease Resistance: Effector AVR2 Associates with BSL1

Diane G.O. Saunders, Susan Breen, Joe Win, Sebastian Schornack, Ingo Hein, Tolga O. Bozkurt, Nicolas Champouret, Vivianne G.A.A. Vleeshouwers, Paul R.J. Birch, Eleanor M. Gilroy, Sophien Kamoun (Lead / Corresponding author)

    Research output: Contribution to journalArticle

    82 Citations (Scopus)

    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 NBLRR
    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.
    Original languageEnglish
    Pages (from-to)3420-3434
    Number of pages14
    JournalPlant Cell
    Volume24
    Issue number8
    Early online date10 Aug 2012
    DOIs
    Publication statusPublished - Aug 2012

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