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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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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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 |
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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 |
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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 |
work_keys_str_mv |
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_version_ |
1792500633418334208 |