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


Journal

The Plant journal : for cell and molecular biology
ISSN: 1365-313X
Titre abrégé: Plant J
Pays: England
ID NLM: 9207397

Informations de publication

Date de publication:
05 2021
Historique:
revised: 15 02 2021
received: 19 11 2020
accepted: 18 02 2021
pubmed: 26 2 2021
medline: 15 12 2021
entrez: 25 2 2021
Statut: ppublish

Résumé

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.

Identifiants

pubmed: 33629439
doi: 10.1111/tpj.15214
doi:

Substances chimiques

Amino Acids 0
Fungal Proteins 0
NLR Proteins 0
Plant Proteins 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

993-1007

Subventions

Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/P016855/1
Pays : United Kingdom

Informations de copyright

© 2021 Society for Experimental Biology and John Wiley & Sons Ltd.

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Auteurs

Beatrice Manser (B)

Department of Plant and Microbial Biology, University of Zurich, Zollikerstrasse 107, Zurich, 8008, Switzerland.

Teresa Koller (T)

Department of Plant and Microbial Biology, University of Zurich, Zollikerstrasse 107, Zurich, 8008, Switzerland.

Coraline Rosalie Praz (CR)

Department of Plant and Microbial Biology, University of Zurich, Zollikerstrasse 107, Zurich, 8008, Switzerland.

Anne C Roulin (AC)

Department of Plant and Microbial Biology, University of Zurich, Zollikerstrasse 107, Zurich, 8008, Switzerland.

Helen Zbinden (H)

Department of Plant and Microbial Biology, University of Zurich, Zollikerstrasse 107, Zurich, 8008, Switzerland.

Sanu Arora (S)

John Innes Centre, Norwich Research Park, Norwich, NR4 7UH, UK.

Burkhard Steuernagel (B)

John Innes Centre, Norwich Research Park, Norwich, NR4 7UH, UK.

Brande B H Wulff (BBH)

John Innes Centre, Norwich Research Park, Norwich, NR4 7UH, UK.

Beat Keller (B)

Department of Plant and Microbial Biology, University of Zurich, Zollikerstrasse 107, Zurich, 8008, Switzerland.

Javier Sánchez-Martín (J)

Department of Plant and Microbial Biology, University of Zurich, Zollikerstrasse 107, Zurich, 8008, Switzerland.

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