Poster
Kaori Oikawa
Iwate Biotechnology Research Center
Kitakami, Iwate, Japan
Koki Fujisaki
Chief Researcher
Iwate Biological Research Center
Kitakami, Iwate, Japan
Motoki Shimizu
Iwate Birotechnology Research Center
Kitakami, Iwate, Japan
Hiromasa Saitoh
Department of Molecular Microbiology, Tokyo University of Agriculture
Setagaya-ku, Tokyo, Japan
Tolga Bozkurt, PhD (he/him/his)
Reader
Imperial College London
London, England, United Kingdom
Stella Cesari (she/her/hers)
PHIM Plant Health Institute, Univ Montpellier, INRAE, CIRAD, Institut Agro, IRD
Montpellier, FRANCE
Thomas Kroj
Plant Health Institute of Montpellier
Montpellier, Languedoc-Roussillon, France
Mark J. Banfield
Group Leader
John Innes Centre
Norwich, England, United Kingdom
Sophien Kamoun
Group leader
The Sainsbury Laboratory
Norwich, England, United Kingdom
Ryohei Terauchi, PhD
Professor
Kyoto University
Muko, Kyoto, Kyoto, Japan
Intracellular nucleotide-binding domain and leucine-rich repeat-containing (NLR) receptors play crucial roles in immunity across multiple domains of life. In plants, a subset of NLRs contain noncanonical integrated domains that are thought to have evolved from host targets of pathogen effectors to serve as pathogen baits. However, the functions of host proteins with similarity to NLR integrated domains and the extent to which they are targeted by pathogen effectors remain largely unknown. Here, we show that the blast fungus effector AVR-Pik binds a subset of related rice proteins containing a heavy metal-associated (HMA) domain, one of the domains that has repeatedly integrated into plant NLR immune receptors. We find that AVR-Pik binding stabilizes the rice small HMA (sHMA) proteins OsHIPP19 and OsHIPP20. Knockout of OsHIPP20 causes enhanced disease resistance towards the blast pathogen, indicating that OsHIPP20 is a susceptibility gene (S-gene). We propose that AVR-Pik has evolved to bind HMA domain proteins and co-opt their function to suppress immunity. Yet this binding carries a trade-off, it triggers immunity in plants carrying NLR receptors with integrated HMA domains.