7B1I

Complex of rice blast (Magnaporthe oryzae) effector protein AVR-PikF with the HMA domain of OsHIPP19 from rice (Oryza sativa)

Summary for 7B1I

• Entry DOI: 10.2210/pdb7b1i/pdb
• Descriptor: OSIGBa0128P10.9 protein, AVR-Pik protein (3 entities in total)
• Functional Keywords: complex, effector, hma domain, rice, rice blast fungus, plant protein
• Biological source: Oryza sativa (Rice); More
• Total number of polymer chains: 2
• Total formula weight: 19194.16

Authors

Maidment, J.H.R.,Franceschetti, M.,Banfield, M.J. (deposition date: 2020-11-24, release date: 2021-02-03, Last modification date: 2024-01-31)

Primary citation

Maidment, J.H.R.,Franceschetti, M.,Maqbool, A.,Saitoh, H.,Jantasuriyarat, C.,Kamoun, S.,Terauchi, R.,Banfield, M.J.
Multiple variants of the fungal effector AVR-Pik bind the HMA domain of the rice protein OsHIPP19, providing a foundation to engineer plant defense.
J.Biol.Chem., 296:100371-100371, 2021

PubMed 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.

PubMed: 33548226
DOI: 10.1016/j.jbc.2021.100371

Experimental method

X-RAY DIFFRACTION (1.9 Å)