Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 119, Issue 43, Pages -Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.2210559119
Keywords
effector; plant immunity; NLR; Exocyst
Categories
Funding
- UK Research and Innovation Biotechnology and Biological Sciences Research Council [BB/P012574, BBS/E/J/000PR9795, BBS/E/J/000PR9777, BB/V015508/1]
- European Research Council [743165]
- John Innes Foundation
- Gatsby Charitable Foundation
- European Commission through the Erasmus+ Programme
- Japan Society for the Promotion of Science [20H05681]
- European Research Council (ERC) [743165] Funding Source: European Research Council (ERC)
Ask authors/readers for more resources
The study reveals the association between the blast fungus Maganaporthe oryzae effector AVR-Pii and rice Exo70 alleles OsExo70F2 and OsExo70F3, which is sensed by the immune receptor pair Pii via an integrated RIN4/NOI domain. The crystal structure of AVR-Pii in complex with OsExo70F2 shows that the effector binds to a conserved hydrophobic pocket in Exo70, defining an effector/target binding interface. This discovery provides new opportunities for engineering disease resistance by manipulating plant exocytosis.
Exocytosis plays an important role in plant-microbe interactions, in both pathogenesis and symbiosis. Exo70 proteins are integral components of the exocyst, an octameric complex that mediates tethering of vesicles to membranes in eukaryotes. Although plant Exo70s are known to be targeted by pathogen effectors, the underpinning molecular mechanisms and the impact of this interaction on infection are poorly understood. Here, we show the molecular basis of the association between the effector AVR-Pii of the blast fungus Maganaporthe oryzae and rice Exo70 alleles OsExo70F2 and OsExo70F3, which is sensed by the immune receptor pair Pii via an integrated RIN4/NOI domain. The crystal structure of AVR-Pii in complex with OsExo70F2 reveals that the effector binds to a conserved hydrophobic pocket in Exo70, defining an effector/target binding interface. Structure-guided and random mutagenesis validates the importance of AVR-Pii residues at the Exo70 binding interface to sustain protein association and disease resistance in rice when challenged with fungal strains expressing effector mutants. Furthermore, the structure of AVR-Pii defines a zinc-finger effector fold (ZiF) distinct from the MAX (Magnaporthe Avrs and ToxB-like) fold previously described for a majority of characterized M. oryzae effectors. Our data suggest that blast fungus ZiF effectors bind a conserved Exo70 interface to manipulate plant exocytosis and that these effectors are also baited by plant immune receptors, pointing to new opportunities for engineering disease resistance.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available