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| Title | The barley MLA13-AVR heterodimer reveals principles for immunoreceptor recognition of RNase-like powdery mildew effectors. |
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| Journal, issue, pages | EMBO J, Vol. 44, Issue 11, Page 3210-3230, Year 2025 |
| Publish date | Feb 13, 2025 |
 Authors | Aaron W Lawson / Andrea Flores-Ibarra / Yu Cao / Chunpeng An / Ulla Neumann / Monika Gunkel / Isabel M L Saur / Jijie Chai / Elmar Behrmann / Paul Schulze-Lefert /   |
| PubMed 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) ...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). We present here the cryo-EM structure of barley MLA13 in complex with its cognate effector AVR-1. The effector adopts an RNase-like fold when bound to MLA13 in planta, similar to crystal structures of other RNase-like AVR effectors unbound to receptors. AVR-1 interacts via its basal loops with MLA13 C-terminal leucine-rich repeats (LRRs) and the central winged helix domain (WHD). Co-expression of structure-guided MLA13 and AVR-1 substitution variants show that the receptor-effector interface plays an essential role in mediating immunity-associated plant cell death. Furthermore, by combining structural information from the MLA13-AVR-1 heterocomplex with sequence alignments of other MLA receptors, we engineered a single amino acid substitution in MLA7 that enables expanded effector detection of AVR-1 and the virulent variant AVR-V2. In contrast to the pentameric conformation of previously reported effector-activated CNL resistosomes, MLA13 was purified and resolved as a stable heterodimer from an in planta expression system. Our study suggests a common structural principle for RNase-like effector binding to MLAs and highlights the utility of structure-guided engineering of plant immune receptors for broadening their pathogen effector recognition capabilities. |
 External links | EMBO J / PubMed:39948409 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.8 Å |
| Structure data | EMDB-50863, PDB-9fyc: |
| Source |
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 Keywords | ANTIFUNGAL PROTEIN / Complex / Apoptosis / Immune receptor / Mildew |
hordeum vulgare (barley)
blumeria graminis (grass mildew)