The stem rust effector protein AvrSr50 escapes Sr50 recognition by a substitution in a single surface‐exposed residue

• Published in: The New phytologist Vol. 234; no. 2; pp. 592 - 606
• Main Authors: Ortiz, Diana, Chen, Jian, Outram, Megan A., Saur, Isabel M.L., Upadhyaya, Narayana M., Mago, Rohit, Ericsson, Daniel J., Cesari, Stella, Chen, Chunhong, Williams, Simon J., Dodds, Peter N.
• Format: Journal Article
• Language: English
• Published: England Wiley Subscription Services, Inc 01-04-2022; Wiley; John Wiley and Sons Inc
• Subjects: Alleles; AvrSr50; Basidiomycota - physiology; Binding; Breeding; Carbohydrates; Colonization; Crystal structure; Deoxyribonucleic acid; Disease Resistance - genetics; DNA; effector evolution; effector structure; Evolution; Genetic diversity; Genetic variation; Homology; Insertion; Life Sciences; Molecular modelling; Mutagenesis; Pathogens; Phytopathology and phytopharmacy; Plant Breeding; Plant Diseases - genetics; Plant resistance; Population genetics; Populations; Proteins; Recognition; Residues; resistance breakdown; Saccharides; Site-directed mutagenesis; Sr50; Stem rust; Stems; Stop codon; Substitutes; Triticum - genetics; Vegetal Biology; Virulence; wheat resistance; resistance breakdown; wheat resistance; effector evolution; AvrSr50; Sr50; effector structure; stem rust
• ISSN: 0028-646X; 1469-8137
• DOI: 10.1111/nph.18011

Summary
Pathogen effectors are crucial players during plant colonisation and infection. Plant resistance mostly relies on effector recognition to activate defence responses. Understanding how effector proteins escape from plant surveillance is important for plant breeding and resistance deployment.
Here we examined the role of genetic diversity of the stem rust (Puccinia graminis f. sp. tritici (Pgt)) AvrSr50 gene in determining recognition by the corresponding wheat Sr50 resistance gene. We solved the crystal structure of a natural variant of AvrSr50 and used site‐directed mutagenesis and transient expression assays to dissect the molecular mechanisms explaining gain of virulence.
We report that AvrSr50 can escape recognition by Sr50 through different mechanisms including DNA insertion, stop codon loss or by amino‐acid variation involving a single substitution of the AvrSr50 surface‐exposed residue Q121. We also report structural homology of AvrSr50 to cupin superfamily members and carbohydrate‐binding modules indicating a potential role in binding sugar moieties.
This study identifies key polymorphic sites present in AvrSr50 alleles from natural stem rust populations that play important roles to escape from Sr50 recognition. This constitutes an important step to better understand Pgt effector evolution and to monitor AvrSr50 variants in natural rust populations.