RT Journal Article
SR Electronic
T1 The blast pathogen effector AVR-Pik binds and stabilizes rice heavy metal-associated (HMA) proteins to co-opt their function in immunity
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2020.12.01.406389
DO 10.1101/2020.12.01.406389
A1 K. Oikawa
A1 K. Fujisaki
A1 M. Shimizu
A1 T. Takeda
A1 H. Saitoh
A1 A. Hirabuchi
A1 Y. Hiraka
A1 A. Białas
A1 T. Langner
A1 R. Kellner
A1 T. O. Bozkurt
A1 S. Cesari
A1 T. Kroj
A1 J. H. R. Maidment
A1 M. J. Banfield
A1 S. Kamoun
A1 R. Terauchi
YR 2020
UL http://biorxiv.org/content/early/2020/12/02/2020.12.01.406389.abstract
AB Plant intracellular nucleotide-binding domain and leucine-rich repeat-containing (NLR) immune receptors have a complex architecture. They can include 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 HMA 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.Competing Interest StatementThe authors have declared no competing interest.