New Recognition Specificity in a Plant Immune Receptor by Molecular Engineering of Its Integrated Domain

Overview

Journal Nat Commun

Specialty Biology

Date 2022 Mar 22

PMID 35314704

Authors

Stella Cesari

Yuxuan Xi

Nathalie Declerck

Veronique Chalvon

Lea Mammri

Martine Pugniere

Corinne Henriquet

Karine de Guillen

Vincent Chochois

Andre Padilla

Thomas Kroj

Affiliations

Soon will be listed here.

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.

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