7QPX
Complex of rice blast (Magnaporthe oryzae) effector protein AVR-PikC with an engineered HMA domain of Pikp-1 (Pikp-SNK-EKE) from rice (Oryza sativa)
Summary for 7QPX
Entry DOI | 10.2210/pdb7qpx/pdb |
Descriptor | Resistance protein Pikp-1, AVR-Pik protein (3 entities in total) |
Functional Keywords | plant immunity, pathogen effector, protein engineering, blast disease, antifungal protein |
Biological source | Oryza sativa Japonica Group (Japanese rice) More |
Total number of polymer chains | 6 |
Total formula weight | 55418.03 |
Authors | Maidment, J.H.R.,Banfield, M.J. (deposition date: 2022-01-05, release date: 2022-06-22, Last modification date: 2024-11-06) |
Primary citation | Maidment, J.H.R.,Shimizu, M.,Bentham, A.R.,Vera, S.,Franceschetti, M.,Longya, A.,Stevenson, C.E.M.,De la Concepcion, J.C.,Bialas, A.,Kamoun, S.,Terauchi, R.,Banfield, M.J. Effector target-guided engineering of an integrated domain expands the disease resistance profile of a rice NLR immune receptor. Elife, 12:-, 2023 Cited by PubMed Abstract: A subset of plant intracellular NLR immune receptors detect effector proteins, secreted by phytopathogens to promote infection, through unconventional integrated domains which resemble the effector's host targets. Direct binding of effectors to these integrated domains activates plant defenses. The rice NLR receptor Pik-1 binds the effector AVR-Pik through an integrated heavy metal-associated (HMA) domain. However, the stealthy alleles AVR-PikC and AVR-PikF avoid interaction with Pik-HMA and evade host defenses. Here, we exploited knowledge of the biochemical interactions between AVR-Pik and its host target, OsHIPP19, to engineer novel Pik-1 variants that respond to AVR-PikC/F. First, we exchanged the HMA domain of Pikp-1 for OsHIPP19-HMA, demonstrating that effector targets can be incorporated into NLR receptors to provide novel recognition profiles. Second, we used the structure of OsHIPP19-HMA to guide the mutagenesis of Pikp-HMA to expand its recognition profile. We demonstrate that the extended recognition profiles of engineered Pikp-1 variants correlate with effector binding in planta and in vitro, and with the gain of new contacts across the effector/HMA interface. Crucially, transgenic rice producing the engineered Pikp-1 variants was resistant to blast fungus isolates carrying AVR-PikC or AVR-PikF. These results demonstrate that effector target-guided engineering of NLR receptors can provide new-to-nature disease resistance in crops. PubMed: 37199729DOI: 10.7554/eLife.81123 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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