New recognition specificity in a plant immune receptor by molecular engineering of its integrated domain

Plant nucleotide-binding and leucine-rich repeat domain proteins (NLRs) are immune sensors that recognize pathogen effectors. Here, we show that molecular engineering of the integrated decoy domain (ID) of an NLR can extend its recognition spectrum to a new effector. We relied for this on detailed knowledge on the recognition of the Magnaporthe oryzae effectors AVR-PikD, AVR-Pia, and AVR1-CO39 by, respectively, the rice NLRs Pikp-1 and RGA5. Both receptors detect their effectors through physical binding to their HMA (Heavy Metal-Associated) IDs. By introducing into RGA5_HMA the AVR-PikD binding residues of Pikp-1_HMA, we create a high-affinity binding surface for this effector. RGA5 variants carrying this engineered binding surface perceive the new ligand, AVR-PikD, and still recognize AVR-Pia and AVR1-CO39 in the model plant N. benthamiana. However, they do not confer extended disease resistance specificity against M. oryzae in transgenic rice plants. Altogether, our study provides a proof of concept for the design of new effector recognition specificities in NLRs through molecular engineering of IDs.

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Main Authors: Cesari, Stella, Xi, Yuxuan, Declerck, Nathalie, Chalvon, Véronique, Mammri, Léa, Pugnière, Martine, Henriquet, Corinne, de Guillen, Karine, Chochois, Vincent, Padilla, André, Kroj, Thomas
Format: article biblioteca
Language:eng
Subjects:Oryza sativa, effecteur moléculaire, plante transgénique, résistance aux maladies, expression des gènes, immunité, Magnaporthe, amélioration des plantes, http://aims.fao.org/aos/agrovoc/c_5438, http://aims.fao.org/aos/agrovoc/c_27506, http://aims.fao.org/aos/agrovoc/c_27619, http://aims.fao.org/aos/agrovoc/c_2328, http://aims.fao.org/aos/agrovoc/c_27527, http://aims.fao.org/aos/agrovoc/c_3802, http://aims.fao.org/aos/agrovoc/c_31827, http://aims.fao.org/aos/agrovoc/c_5956,
Online Access:http://agritrop.cirad.fr/606400/
http://agritrop.cirad.fr/606400/1/ID606400.pdf
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spelling dig-cirad-fr-6064002024-01-29T19:02:45Z http://agritrop.cirad.fr/606400/ http://agritrop.cirad.fr/606400/ New recognition specificity in a plant immune receptor by molecular engineering of its integrated domain. Cesari Stella, Xi Yuxuan, Declerck Nathalie, Chalvon Véronique, Mammri Léa, Pugnière Martine, Henriquet Corinne, de Guillen Karine, Chochois Vincent, Padilla André, Kroj Thomas. 2022. Nature Communications, 13:1524, 13 p.https://doi.org/10.1038/s41467-022-29196-6 <https://doi.org/10.1038/s41467-022-29196-6> New recognition specificity in a plant immune receptor by molecular engineering of its integrated domain Cesari, Stella Xi, Yuxuan Declerck, Nathalie Chalvon, Véronique Mammri, Léa Pugnière, Martine Henriquet, Corinne de Guillen, Karine Chochois, Vincent Padilla, André Kroj, Thomas eng 2022 Nature Communications Oryza sativa effecteur moléculaire plante transgénique résistance aux maladies expression des gènes immunité Magnaporthe amélioration des plantes http://aims.fao.org/aos/agrovoc/c_5438 http://aims.fao.org/aos/agrovoc/c_27506 http://aims.fao.org/aos/agrovoc/c_27619 http://aims.fao.org/aos/agrovoc/c_2328 http://aims.fao.org/aos/agrovoc/c_27527 http://aims.fao.org/aos/agrovoc/c_3802 http://aims.fao.org/aos/agrovoc/c_31827 http://aims.fao.org/aos/agrovoc/c_5956 Plant nucleotide-binding and leucine-rich repeat domain proteins (NLRs) are immune sensors that recognize pathogen effectors. Here, we show that molecular engineering of the integrated decoy domain (ID) of an NLR can extend its recognition spectrum to a new effector. We relied for this on detailed knowledge on the recognition of the Magnaporthe oryzae effectors AVR-PikD, AVR-Pia, and AVR1-CO39 by, respectively, the rice NLRs Pikp-1 and RGA5. Both receptors detect their effectors through physical binding to their HMA (Heavy Metal-Associated) IDs. By introducing into RGA5_HMA the AVR-PikD binding residues of Pikp-1_HMA, we create a high-affinity binding surface for this effector. RGA5 variants carrying this engineered binding surface perceive the new ligand, AVR-PikD, and still recognize AVR-Pia and AVR1-CO39 in the model plant N. benthamiana. However, they do not confer extended disease resistance specificity against M. oryzae in transgenic rice plants. Altogether, our study provides a proof of concept for the design of new effector recognition specificities in NLRs through molecular engineering of IDs. article info:eu-repo/semantics/article Journal Article info:eu-repo/semantics/publishedVersion http://agritrop.cirad.fr/606400/1/ID606400.pdf text cc_by info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/4.0/ https://doi.org/10.1038/s41467-022-29196-6 10.1038/s41467-022-29196-6 info:eu-repo/semantics/altIdentifier/doi/10.1038/s41467-022-29196-6 info:eu-repo/semantics/altIdentifier/purl/https://doi.org/10.1038/s41467-022-29196-6 info:eu-repo/grantAgreement///ANR-15-CE20-0007//(FRA) Récepteurs immunitaires de type NLR pour des résistances plus durables chez les céréales/ImmuneReceptor info:eu-repo/grantAgreement///ANR-10-INBS-0005//(FRA) Infrastructure Française pour la Biologie Structurale Intégrée/FRISBI
institution CIRAD FR
collection DSpace
country Francia
countrycode FR
component Bibliográfico
access En linea
databasecode dig-cirad-fr
tag biblioteca
region Europa del Oeste
libraryname Biblioteca del CIRAD Francia
language eng
topic Oryza sativa
effecteur moléculaire
plante transgénique
résistance aux maladies
expression des gènes
immunité
Magnaporthe
amélioration des plantes
http://aims.fao.org/aos/agrovoc/c_5438
http://aims.fao.org/aos/agrovoc/c_27506
http://aims.fao.org/aos/agrovoc/c_27619
http://aims.fao.org/aos/agrovoc/c_2328
http://aims.fao.org/aos/agrovoc/c_27527
http://aims.fao.org/aos/agrovoc/c_3802
http://aims.fao.org/aos/agrovoc/c_31827
http://aims.fao.org/aos/agrovoc/c_5956
Oryza sativa
effecteur moléculaire
plante transgénique
résistance aux maladies
expression des gènes
immunité
Magnaporthe
amélioration des plantes
http://aims.fao.org/aos/agrovoc/c_5438
http://aims.fao.org/aos/agrovoc/c_27506
http://aims.fao.org/aos/agrovoc/c_27619
http://aims.fao.org/aos/agrovoc/c_2328
http://aims.fao.org/aos/agrovoc/c_27527
http://aims.fao.org/aos/agrovoc/c_3802
http://aims.fao.org/aos/agrovoc/c_31827
http://aims.fao.org/aos/agrovoc/c_5956
spellingShingle Oryza sativa
effecteur moléculaire
plante transgénique
résistance aux maladies
expression des gènes
immunité
Magnaporthe
amélioration des plantes
http://aims.fao.org/aos/agrovoc/c_5438
http://aims.fao.org/aos/agrovoc/c_27506
http://aims.fao.org/aos/agrovoc/c_27619
http://aims.fao.org/aos/agrovoc/c_2328
http://aims.fao.org/aos/agrovoc/c_27527
http://aims.fao.org/aos/agrovoc/c_3802
http://aims.fao.org/aos/agrovoc/c_31827
http://aims.fao.org/aos/agrovoc/c_5956
Oryza sativa
effecteur moléculaire
plante transgénique
résistance aux maladies
expression des gènes
immunité
Magnaporthe
amélioration des plantes
http://aims.fao.org/aos/agrovoc/c_5438
http://aims.fao.org/aos/agrovoc/c_27506
http://aims.fao.org/aos/agrovoc/c_27619
http://aims.fao.org/aos/agrovoc/c_2328
http://aims.fao.org/aos/agrovoc/c_27527
http://aims.fao.org/aos/agrovoc/c_3802
http://aims.fao.org/aos/agrovoc/c_31827
http://aims.fao.org/aos/agrovoc/c_5956
Cesari, Stella
Xi, Yuxuan
Declerck, Nathalie
Chalvon, Véronique
Mammri, Léa
Pugnière, Martine
Henriquet, Corinne
de Guillen, Karine
Chochois, Vincent
Padilla, André
Kroj, Thomas
New recognition specificity in a plant immune receptor by molecular engineering of its integrated domain
description Plant nucleotide-binding and leucine-rich repeat domain proteins (NLRs) are immune sensors that recognize pathogen effectors. Here, we show that molecular engineering of the integrated decoy domain (ID) of an NLR can extend its recognition spectrum to a new effector. We relied for this on detailed knowledge on the recognition of the Magnaporthe oryzae effectors AVR-PikD, AVR-Pia, and AVR1-CO39 by, respectively, the rice NLRs Pikp-1 and RGA5. Both receptors detect their effectors through physical binding to their HMA (Heavy Metal-Associated) IDs. By introducing into RGA5_HMA the AVR-PikD binding residues of Pikp-1_HMA, we create a high-affinity binding surface for this effector. RGA5 variants carrying this engineered binding surface perceive the new ligand, AVR-PikD, and still recognize AVR-Pia and AVR1-CO39 in the model plant N. benthamiana. However, they do not confer extended disease resistance specificity against M. oryzae in transgenic rice plants. Altogether, our study provides a proof of concept for the design of new effector recognition specificities in NLRs through molecular engineering of IDs.
format article
topic_facet Oryza sativa
effecteur moléculaire
plante transgénique
résistance aux maladies
expression des gènes
immunité
Magnaporthe
amélioration des plantes
http://aims.fao.org/aos/agrovoc/c_5438
http://aims.fao.org/aos/agrovoc/c_27506
http://aims.fao.org/aos/agrovoc/c_27619
http://aims.fao.org/aos/agrovoc/c_2328
http://aims.fao.org/aos/agrovoc/c_27527
http://aims.fao.org/aos/agrovoc/c_3802
http://aims.fao.org/aos/agrovoc/c_31827
http://aims.fao.org/aos/agrovoc/c_5956
author Cesari, Stella
Xi, Yuxuan
Declerck, Nathalie
Chalvon, Véronique
Mammri, Léa
Pugnière, Martine
Henriquet, Corinne
de Guillen, Karine
Chochois, Vincent
Padilla, André
Kroj, Thomas
author_facet Cesari, Stella
Xi, Yuxuan
Declerck, Nathalie
Chalvon, Véronique
Mammri, Léa
Pugnière, Martine
Henriquet, Corinne
de Guillen, Karine
Chochois, Vincent
Padilla, André
Kroj, Thomas
author_sort Cesari, Stella
title New recognition specificity in a plant immune receptor by molecular engineering of its integrated domain
title_short New recognition specificity in a plant immune receptor by molecular engineering of its integrated domain
title_full New recognition specificity in a plant immune receptor by molecular engineering of its integrated domain
title_fullStr New recognition specificity in a plant immune receptor by molecular engineering of its integrated domain
title_full_unstemmed New recognition specificity in a plant immune receptor by molecular engineering of its integrated domain
title_sort new recognition specificity in a plant immune receptor by molecular engineering of its integrated domain
url http://agritrop.cirad.fr/606400/
http://agritrop.cirad.fr/606400/1/ID606400.pdf
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