ArticleThe Journal of biological chemistry
Multiple variants of the fungal effector AVR-Pik bind the HMA domain of the rice protein OsHIPP19, providing a foundation to engineer plant defense.
Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed.
- Pathogenicity and virulence of the blast fungusVirulence · 2026Review
- Engineering plant tandem kinase immune receptors expands effector recognition profiles.Science advances · 2026Article
- Structure-informed engineering of plant-microbe interactions.The Plant journal : for cell and molecular biology · 2026Review
- Two folds, many faces: The Magnaporthe oryzae MAX effector AVR-Pia targets novel rice HMA domain-containing proteins.PLoS pathogens · 2026Article
- Engineering an Exo70 integrated domain of a barley NLR for improved blast resistance.The Plant cell · 2026Article
- How to frustrate a plant pathogen.The Plant journal : for cell and molecular biology · 2026Review
- 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
- The VlMYB149-VlHIPP30 Regulatory Module Enhances Grapevine Resistance to Botrytis cinerea by Activating the Antioxidant System and Copper Metabolism.Molecular plant pathology · 2026Article
- A binary-distributed effector modulates fungal host preference for drosophilids by targeting a lineage-specific immune factor.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- The Magnaporthe oryzae effector Pwl2 alters HIPP43 localization to suppress host immunity.The Plant cell · 2025Article
- The resistance awakens: Diversity at the DNA, RNA, and protein levels informs engineering of plant immune receptors from Arabidopsis to crops.The Plant cell · 2025Review
- Structure-guided insights into the biology of fungal effectors.The New phytologist · 2025Review
- Status on Genetic Resistance to Rice Blast Disease in the Post-Genomic Era.Plants (Basel, Switzerland) · 2025Review
- Live cell imaging of plant infection provides new insight into the biology of pathogenesis by the rice blast fungus Magnaporthe oryzae.Journal of microscopy · 2025Review
- All Roads Lead to Rome: Pathways to Engineering Disease Resistance in Plants.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- CRISPR-mediated genome editing of wheat for enhancing disease resistance.Frontiers in genome editing · 2025Review
- Exploring effector protein dynamics and natural fungicidal potential in rice blast pathogen Magnaporthe oryzae.PloS one · 2025Article
- Mechanism of Action ofPlants (Basel, Switzerland) · 2024Article
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8 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Microbial plant pathogens secrete effector proteins, which manipulate the host to promote infection. Effectors can be recognized by plant intracellular nucleotide-binding leucine-rich repeat (NLR) receptors, initiating an immune response. The AVR-Pik effector from the rice blast fungus Magnaporthe oryzae is recognized by a pair of rice NLR receptors, Pik-1 and Pik-2. Pik-1 contains a noncanonical integrated heavy-metal-associated (HMA) domain, which directly binds AVR-Pik to activate plant defenses. The host targets of AVR-Pik are also HMA-domain-containing proteins, namely heavy-metal-associated isoprenylated plant proteins (HIPPs) and heavy-metal-associated plant proteins (HPPs). Here, we demonstrate that one of these targets interacts with a wider set of AVR-Pik variants compared with the Pik-1 HMA domains. We define the biochemical and structural basis of the interaction between AVR-Pik and OsHIPP19 and compare the interaction to that formed with the HMA domain of Pik-1. Using analytical gel filtration and surface plasmon resonance, we show that multiple AVR-Pik variants, including the stealthy variants AVR-PikC and AVR-PikF, which do not interact with any characterized Pik-1 alleles, bind to OsHIPP19 with nanomolar affinity. The crystal structure of OsHIPP19 in complex with AVR-PikF reveals differences at the interface that underpin high-affinity binding of OsHIPP19-HMA to a wider set of AVR-Pik variants than achieved by the integrated HMA domain of Pik-1. Our results provide a foundation for engineering the HMA domain of Pik-1 to extend binding to currently unrecognized AVR-Pik variants and expand disease resistance in rice to divergent pathogen strains.
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