PR1?mediated defence via C?terminal peptide release is targeted by a fungal pathogen effector

The effector SnTox3 from Parastagonospora nodorum elicits a strong necrotic response in susceptible wheat and also interacts with pathogenesis-related protein 1 (TaPR-1), although the function of this interaction disease is unclear. Here, we dissect TaPR1 by studying SnTox3–TaPR1 demonstrate dual functionality SnTox3. We utilized site-directed mutagenesis to identify an variant, SnTox3P173S, that was unable interact yeast-two-hybrid assays. Additionally, using recombinant proteins established novel protein-mediated phenotyping assay allowing functional studies be undertaken wheat. Wheat leaves infiltrated showed significantly less compared control leaves, correlating increase defence gene expression. This activity dependent on release TaCAPE1 peptide embedded within unidentified serine protease. priming compromised but not noninteracting variant prevents vitro. independently functions induce necrosis through recognition Snn3 suppresses host direct proteins. Importantly, study advances our understanding role PR1 host–microbe interactions as inducers signalling.