Structural basis of pathogen recognition by an integrated HMA domain in a plant NLR immune receptor

Maqbool, A., Saitoh, H., Franceschetti, M., Stevenson, C. E M, Uemura, A., Kanzaki, H., Kamoun, S. ORCID: https://orcid.org/0000-0002-0290-0315, Terauchi, R. and Banfield, M. J. (2015) Structural basis of pathogen recognition by an integrated HMA domain in a plant NLR immune receptor. eLife, 4. ISSN 2050-084X

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Abstract

Plants have evolved intracellular immune receptors to detect pathogen proteins known as effectors. How these immune receptors detect effectors remains poorly understood. Here we describe the structural basis for direct recognition of AVR-Pik, an effector from the rice blast pathogen, by the rice intracellular NLR immune receptor Pik. AVR-PikD binds a dimer of the Pikp-1 HMA integrated domain with nanomolar affinity. The crystal structure of the Pikp-HMA/AVR-PikD complex enabled design of mutations to alter protein interaction in yeast and in vitro, and perturb effector-mediated response both in a rice cultivar containing Pikp and upon expression of AVR-PikD and Pikp in the model plant Nicotiana benthamiana. These data reveal the molecular details of a recognition event, mediated by a novel integrated domain in an NLR, which initiates a plant immune response and resistance to rice blast disease. Such studies underpin novel opportunities for engineering disease resistance to plant pathogens in staple food crops.

Item Type:	Article
Faculty \ School:	Faculty of Science > The Sainsbury Laboratory Faculty of Science > School of Biological Sciences
UEA Research Groups:	Faculty of Science > Research Groups > Plant Sciences
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	Pure Connector
Date Deposited:	01 Jun 2016 12:00
Last Modified:	22 Oct 2022 01:13
URI:	https://ueaeprints.uea.ac.uk/id/eprint/59170
DOI:	10.7554/eLife.08709

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