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

• Published in: Nature communications Vol. 13; no. 1; p. 1524
• 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: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 21.03.2022; Nature Publishing Group; Nature Portfolio
• Subjects: 631/449/1659; 631/449/2169/2107; 631/449/2675; 631/449/447/2311; 82/103; 82/111; Binding; Disease resistance; Effectors; Engineering; Heavy metals; Host-Pathogen Interactions; Humanities and Social Sciences; Immune response; Leucine; Life Sciences; Magnaporthe; multidisciplinary; NLR Proteins - metabolism; Nucleotides; Oryza - metabolism; Pathogens; Phytopathology and phytopharmacy; Plant Diseases - genetics; Plant Proteins - metabolism; Plants, Genetically Modified - metabolism; Proteins; Receptors; Receptors, Immunologic - metabolism; Recognition; Rice; Science; Science (multidisciplinary); Transgenic plants; Vegetal Biology; Récepteur immunitaire
• ISSN: 2041-1723; 2041-1723
• DOI: 10.1038/s41467-022-29196-6

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. Plant NLR proteins trigger immune responses upon recognition of pathogen effectors. Here the authors show that the integrated decoy domain of the rice NLR RGA5 can be engineered to trigger immune responses upon binding a non-cognate effector.