ArticlePLoS pathogens2021
The allelic rice immune receptor Pikh confers extended resistance to strains of the blast fungus through a single polymorphism in the effector binding interface.
Article in PLoS pathogens, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 62 citations in OpenAlex.
- Molecular Bases and Genetic Design of Rice Disease Resistance for Optimized Yield and Sustainable Agriculture.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Structure-informed engineering of plant-microbe interactions.The Plant journal : for cell and molecular biology · 2026Review
- Pathogenicity Analysis and Molecular Characterization of ThreeMicroorganisms · 2026Article
- Precision Editing of NLRS Improves Effector Recognition for Enhanced Disease Resistance.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- HIPPs of all trades: insights from pathogens on the function of HMA proteins at plasmodesmata.Journal of experimental botany · 2026Review
- Structure-guided insights into the biology of fungal effectors.The New phytologist · 2025Review
- Helper NLR immune protein NRC3 evolved to evade inhibition by a cyst nematode virulence effector.PLoS genetics · 2025Article
- Directed Evolution of a Plant Immune Receptor for Broad Spectrum Effector Recognition.bioRxiv : the preprint server for biology · 2025Article
- Review
- Refinement of rice blast disease resistance QTLs and gene networks through meta-QTL analysis.Scientific reports · 2024Article
- Bioengineering a plant NLR immune receptor with a robust binding interface toward a conserved fungal pathogen effector.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Zinc-finger (ZiF) fold secreted effectors form a functionally diverse family across lineages of the blast fungus Magnaporthe oryzae.PLoS pathogens · 2024Article
- Development of an NLR-ID Toolkit and Identification of Novel Disease-Resistance Genes in Soybean.Plants (Basel, Switzerland) · 2024Article
- Magnaporthe oryzae effector AvrPik-D targets a transcription factor WG7 to suppress rice immunity.Rice (New York, N.Y.) · 2024Article
- The Molecular Docking of MAX Fungal Effectors with Plant HMA Domain-Binding Proteins.International journal of molecular sciences · 2023Article
- Resistance that stacks up: engineering rust and mildew disease control in the cereal crops wheat and barley.Plant biotechnology journal · 2023Review
- Allelic compatibility in plant immune receptors facilitates engineering of new effector recognition specificities.The Plant cell · 2023Article
- Does a Similar 3D Structure Mean a Similar Folding Pathway? The Presence of a C-TerminalMolecules (Basel, Switzerland) · 2023Article
- Article
- Structural mechanism of heavy metal-associated integrated domain engineering of paired nucleotide-binding and leucine-rich repeat proteins in rice.Frontiers in plant science · 2023Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 4 countries.
Funding
Abstract
Arms race co-evolution drives rapid adaptive changes in pathogens and in the immune systems of their hosts. Plant intracellular NLR immune receptors detect effectors delivered by pathogens to promote susceptibility, activating an immune response that halts colonization. As a consequence, pathogen effectors evolve to escape immune recognition and are highly variable. In turn, NLR receptors are one of the most diverse protein families in plants, and this variability underpins differential recognition of effector variants. The molecular mechanisms underlying natural variation in effector recognition by NLRs are starting to be elucidated. The rice NLR pair Pik-1/Pik-2 recognizes AVR-Pik effectors from the blast fungus Magnaporthe oryzae, triggering immune responses that limit rice blast infection. Allelic variation in a heavy metal associated (HMA) domain integrated in the receptor Pik-1 confers differential binding to AVR-Pik variants, determining resistance specificity. Previous mechanistic studies uncovered how a Pik allele, Pikm, has extended recognition to effector variants through a specialized HMA/AVR-Pik binding interface. Here, we reveal the mechanistic basis of extended recognition specificity conferred by another Pik allele, Pikh. A single residue in Pikh-HMA increases binding to AVR-Pik variants, leading to an extended effector response in planta. The crystal structure of Pikh-HMA in complex with an AVR-Pik variant confirmed that Pikh and Pikm use a similar molecular mechanism to extend their pathogen recognition profile. This study shows how different NLR receptor alleles functionally converge to extend recognition specificity to pathogen effectors.
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