Ascurra, Yerisf C. Torres, Zhang, Lisha, Toghani, Amirali, Hua, Chenlei, Rangegowda, Nandeesh Jalahalli, Posbeyikian, Andres, Pai, Hsuan, Lin, Xiao, Wolters, Pieter J., Wouters, Doret, de Blok, Reinhoud, Steigenga, Niels, Paillart, Maxence J. M., Visser, Richard G. F., Kamoun, Sophien ORCID: https://orcid.org/0000-0002-0290-0315, Nürnberger, Thorsten and Vleeshouwers, Vivianne G. A. A. (2023) Functional diversification of a wild potato immune receptor at its center of origin. Science, 381 (6660). pp. 891-897. ISSN 0036-8075
Full text not available from this repository. (Request a copy)Abstract
Plant cell surface pattern recognition receptors (PRRs) and intracellular immune receptors cooperate to provide immunity to microbial infection. Both receptor families have coevolved at an accelerated rate, but the evolution and diversification of PRRs is poorly understood. We have isolated potato surface receptor Pep-13 receptor unit (PERU) that senses Pep-13, a conserved immunogenic peptide pattern from plant pathogenic Phytophthora species. PERU, a leucine-rich repeat receptor kinase, is a bona fide PRR that binds Pep-13 and enhances immunity to Phytophthora infestans infection. Diversification in ligand binding specificities of PERU can be traced to sympatric wild tuber-bearing Solanum populations in the Central Andes. Our study reveals the evolution of cell surface immune receptor alleles in wild potato populations that recognize ligand variants not recognized by others.
Item Type: | Article |
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Additional Information: | Publisher Copyright: © 2023 American Association for the Advancement of Science. All rights reserved. |
Uncontrolled Keywords: | general ,/dk/atira/pure/subjectarea/asjc/1000 |
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: | |
Depositing User: | LivePure Connector |
Date Deposited: | 03 Dec 2024 01:35 |
Last Modified: | 03 Dec 2024 01:35 |
URI: | https://ueaeprints.uea.ac.uk/id/eprint/97864 |
DOI: | 10.1126/science.adg5261 |
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