The barley MLA13-AVR_A13 heterodimer reveals principles for immunoreceptor recognition of RNase-like powdery mildew effectors.

ABSTRACT: Co-evolution between cereals and pathogenic grass powdery mildew fungi is exemplified by sequence diversification of an allelic series of barley resistance genes encoding Mildew Locus A (MLA) nucleotide-binding leucine-rich repeat (NLR) immunoreceptors with an N-terminal coiled-coil domain (CNLs). Each immunoreceptor recognises a matching, strain-specific powdery mildew effector encoded by an avirulence gene (AVR_a). We present here the cryo-EM structure of barley MLA13 in complex with its cognate effector AVR_A13-1. The effector adopts an RNase-like fold when bound to MLA13 in planta, similar to crystal structures of other RNase-like AVR_A effectors unbound to receptors. AVR_A13-1 interacts via its basal loops with MLA13 C-terminal leucine-rich repe

SUBMITTER: Lawson AW 

PROVIDER: S-EPMC12130304 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature