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

Stella Cesari (), Yuxuan Xi, Nathalie Declerck, Véronique Chalvon, Léa Mammri, Martine Pugnière, Corinne Henriquet, Karine Guillen, Vincent Chochois, André Padilla and Thomas Kroj ()
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Stella Cesari: PHIM Plant Health Institute, Univ. Montpellier, INRAE, CIRAD, Institut Agro, IRD
Yuxuan Xi: PHIM Plant Health Institute, Univ. Montpellier, INRAE, CIRAD, Institut Agro, IRD
Nathalie Declerck: PHIM Plant Health Institute, Univ. Montpellier, INRAE, CIRAD, Institut Agro, IRD
Véronique Chalvon: PHIM Plant Health Institute, Univ. Montpellier, INRAE, CIRAD, Institut Agro, IRD
Léa Mammri: CBS, Univ. Montpellier, CNRS, INSERM
Martine Pugnière: IRCM, Institut de Recherche en Cancérologie de Montpellier, INSERM U1194, Université de Montpellier, Institut Régional du Cancer de Montpellier
Corinne Henriquet: IRCM, Institut de Recherche en Cancérologie de Montpellier, INSERM U1194, Université de Montpellier, Institut Régional du Cancer de Montpellier
Karine Guillen: CBS, Univ. Montpellier, CNRS, INSERM
Vincent Chochois: Qualisud, Univ. Montpellier, Avignon Université, CIRAD, Institut Agro, Université de La Réunion
André Padilla: CBS, Univ. Montpellier, CNRS, INSERM
Thomas Kroj: PHIM Plant Health Institute, Univ. Montpellier, INRAE, CIRAD, Institut Agro, IRD

Nature Communications, 2022, vol. 13, issue 1, 1-13

Abstract: Abstract 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.

Date: 2022
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DOI: 10.1038/s41467-022-29196-6

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