Science Advances | VOL. 8

Pathogen effector AvrSr35 triggers Sr35 resistosome assembly via a direct recognition mechanism

Publication Date Sep 9, 2022


Nucleotide-binding, leucine-rich repeat receptors (NLRs) perceive pathogen effectors to trigger plant immunity. The direct recognition mechanism of pathogen effectors by coiled-coil NLRs (CNLs) remains unclear. We demonstrate that the Triticum monococcum CNL Sr35 directly recognizes the pathogen effector AvrSr35 from Puccinia graminis f. sp . tritici and report a cryo–electron microscopy structure of Sr35 resistosome and a crystal structure of AvrSr35. We show that AvrSr35 forms homodimers that are disassociated into monomers upon direct recognition by the leucine-rich repeat domain of Sr35, which induces Sr35 resistosome assembly and the subsequent immune response. The first 20 amino-terminal residues of Sr35 are indispensable for immune signaling but not for plasma membrane association. Our findings reveal the direct recognition and activation mechanism of a plant CNL and provide insights into biochemical function of Sr35 resistosome.


Nucleotide-binding, Leucine-rich Repeat Receptors Pathogen Effector Direct Recognition Leucine-rich Repeat Receptors Leucine-rich Repeat Recognition Mechanism Subsequent Response Direct Activation Cryo Electron Microscopy Structure Plasma Membrane Association

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