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Protein engineering expands the effector recognition profile of a rice NLR immune receptor

2019-04-16

Abstract excerpt

Plant NLR receptors detect pathogen effectors and initiate an immune response. Since their discovery, NLRs have been the focus of protein engineering to improve disease resistance. However, this has proven challenging, in part due to their narrow response specificity. Here, we used structure-guided engineering to expand the response profile of the rice NLR Pikp to variants of the rice blast pathogen effector AVR-P...

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Identifiers and source

Literature Corpus work
10a6ce22-c312-543a-afbc-27cb488b7c80
DOI
10.1101/611152
Open publication

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Protein engineering expands the effector recognition profile of a rice NLR immune receptorDOI 10.1101/611152
Effector target-guided engineering of an integrated domain expands the disease resistance profile of a rice NLR immune receptorSemantic proximity
Bioengineering a plant NLR immune receptor with a robust binding interface towards a conserved fungal pathogen effectorSemantic proximity
The allelic rice immune receptor Pikh confers extended resistance to strains of the blast fungus through a single polymorphism in the effector binding interfaceSemantic proximity
The allelic rice immune receptor Pikh confers extended resistance to strains of the blast fungus through a single polymorphism in the effector binding interface.Semantic proximity
Two NLR immune receptors acquired high-affinity binding to a fungal effector through convergent evolution of their integrated domain.Semantic proximity
Cross-reactivity of a rice NLR immune receptor to distinct effectors from the blast pathogen leads to partial disease resistanceSemantic proximity
Computational design of <i>de novo</i> integrated domains enables rational control of pathogen effector recognition in plant NLR immune receptorsSemantic proximity
Allelic compatibility in plant immune receptors facilitates engineering of new effector recognition specificitiesSemantic proximity
The Piks allele of the NLR immune receptor Pik breaks the recognition of AvrPik effectors of rice blast fungus.Semantic proximity
Multiple variants of the blast fungus effector AVR-Pik bind the HMA domain of the rice protein OsHIPP19 with high affinitySemantic proximity
Allelic compatibility in plant immune receptors facilitates engineering of new effector recognition specificities.Semantic proximity
Multiple variants of the fungal effector AVR-Pik bind the HMA domain of the rice protein OsHIPP19, providing a foundation to engineer plant defense.Semantic proximity
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