Identification of specificity-defining amino acids of the wheat immune receptor Pm2 and powdery mildew effector AvrPm2

Autor: Manser, Beatrice, Koller, Teresa, Praz, Coraline Rosalie, Roulin, Anne C, Zbinden, Helen, Arora, Sanu, Steuernagel, Burkhard, Wulff, Brande B H, Keller, Beat, Sánchez‐Martín, Javier
Přispěvatelé: University of Zurich, Keller, Beat, Sánchez‐Martín, Javier
Rok vydání: 2021
Předmět:
0106 biological sciences
0301 basic medicine
Aegilops
Blumeria graminis
Nicotiana benthamiana
NLR Proteins
Plant Science
Immune receptor
580 Plants (Botany)
01 natural sciences
Epitope
UFSP13-7 Evolution in Action: From Genomes to Ecosystems
1307 Cell Biology
Fungal Proteins
03 medical and health sciences
Immune system
10126 Department of Plant and Microbial Biology
1311 Genetics
Ascomycota
1110 Plant Science
Tobacco
Genetics
Aegilops tauschii
Plant Immunity
10211 Zurich-Basel Plant Science Center
Amino Acids
Alleles
Triticum
Disease Resistance
Plant Diseases
Plant Proteins
2. Zero hunger
chemistry.chemical_classification
biology
Effector
food and beverages
Genetic Variation
Cell Biology
biology.organism_classification
Amino acid
030104 developmental biology
chemistry
Host-Pathogen Interactions
Mutation
010606 plant biology & botany
Zdroj: The Plant journal : for cell and molecular biologyREFERENCES. 106(4)
ISSN: 1365-313X
Popis: Plant nucleotide-binding leucine-rich repeat receptors (NLRs) act as intracellular sensors for pathogen-derived effector proteins and trigger an immune response, frequently resulting in the hypersensitive cell death response (HR) of the infected host cell. The wheat (Triticum aestivum) NLR Pm2 confers resistance against the fungal pathogen Blumeria graminis f. sp. tritici (Bgt) if the isolate contains the specific RNase-like effector AvrPm2. We identified and isolated seven new Pm2 alleles (Pm2e-i) in the wheat D-genome ancestor Aegilops tauschii and two new natural AvrPm2 haplotypes from Bgt. Upon transient co-expression in Nicotiana benthamiana, we observed a variant-specific HR of the Pm2 variants Pm2a and Pm2i towards AvrPm2 or its homolog from the AvrPm2 effector family, BgtE-5843, respectively. Through the introduction of naturally occurring non-synonymous single nucleotide polymorphisms and structure-guided mutations, we identified single amino acids in both the wheat NLR Pm2 and the fungal effector proteins AvrPm2 and BgtE-5843 responsible for the variant-specific HR of the Pm2 variants. Exchanging these amino acids led to a modified HR of the Pm2-AvrPm2 interaction and allowed the identification of the effector head epitope, a 20-amino-acid long unit of AvrPm2 involved in the HR. Swapping of the AvrPm2 head epitope to the non-HR-triggering AvrPm2 family member BgtE-5846 led to gain of a HR by Pm2a. Our study presents a molecular approach to identify crucial effector surface structures involved in the HR and demonstrates that natural and induced diversity in an immune receptor and its corresponding effectors can provide the basis for understanding and modifying NLR-effector specificity.
Databáze: OpenAIRE
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