Imperial College London
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Dr Tolga Bozkurt

Faculty of Natural Sciences, Department of Life Sciences

Reader in Molecular Plant-Microbe
 
 
 
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Contact

 

+44 (0)20 7594 5381o.bozkurt

 
 
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Location

 

6167Sir Alexander Fleming BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Oikawa:2020:10.1101/2020.12.01.406389,
author = {Oikawa, K and Fujisaki, K and Shimizu, M and Takeda, T and Nemoto, K and Saitoh, H and Hirabuchi, A and Hiraka, Y and Miyaji, N and Biaas, A and Langner, T and Kellner, R and Bozkurt, TO and Cesari, S and Kroj, T and Banfield, MJ and Kamoun, S and Terauchi, R},
doi = {10.1101/2020.12.01.406389},
title = {The blast pathogen effector AVR-Pik binds and stabilizes rice heavy metal-associated (HMA) proteins to co-opt their function in immunity},
url = {http://dx.doi.org/10.1101/2020.12.01.406389},
year = {2020}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - <jats:title>Abstract</jats:title><jats:p>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<jats:italic>OsHIPP20</jats:italic>causes enhanced disease resistance towards the blast pathogen, indicating that<jats:italic>OsHIPP20</jats:italic>is a susceptibility gene (<jats:italic>S</jats:italic>-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.</jats:p><jats:sec><jats:title>Significance Statement</jats:title><jats:p>Rice blast disease, caused by the fungus<jats:italic>Magnaporthe oryzae</jats:italic>, is one of the most devastating diseases of rice. Therefore, understanding the mechanisms of blast fungus infection and resistance of rice against the disease is important for global food security. In this study, we show that the<jats:italic>M. oryzae</jats:italic>effector protein AVR-PikD binds rice sHMA proteins and stabilizes them, presumably to enhance pathogen infection. We show that loss-of-function mutants in
AU  - Oikawa,K
AU  - Fujisaki,K
AU  - Shimizu,M
AU  - Takeda,T
AU  - Nemoto,K
AU  - Saitoh,H
AU  - Hirabuchi,A
AU  - Hiraka,Y
AU  - Miyaji,N
AU  - Biaas,A
AU  - Langner,T
AU  - Kellner,R
AU  - Bozkurt,TO
AU  - Cesari,S
AU  - Kroj,T
AU  - Banfield,MJ
AU  - Kamoun,S
AU  - Terauchi,R
DO  - 10.1101/2020.12.01.406389
PY  - 2020///
TI  - The blast pathogen effector AVR-Pik binds and stabilizes rice heavy metal-associated (HMA) proteins to co-opt their function in immunity
UR  - http://dx.doi.org/10.1101/2020.12.01.406389
ER  -
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