Structural signatures in EPR3 define a unique class of plant carbohydrate receptors

Jaslyn E. M. M. Wong, Kira Gysel, Thea G. Birkefeldt, Maria Vinther, Artur Muszyński, Parastoo Azadi, Nick S. Laursen, John T. Sullivan, Clive W. Ronson, Jens Stougaard and Kasper R. Andersen ()
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Jaslyn E. M. M. Wong: Aarhus University
Kira Gysel: Aarhus University
Thea G. Birkefeldt: Aarhus University
Maria Vinther: Aarhus University
Artur Muszyński: University of Georgia
Parastoo Azadi: University of Georgia
Nick S. Laursen: Aarhus University
John T. Sullivan: University of Otago
Clive W. Ronson: University of Otago
Jens Stougaard: Aarhus University
Kasper R. Andersen: Aarhus University

Nature Communications, 2020, vol. 11, issue 1, 1-8

Abstract: Abstract Receptor-mediated perception of surface-exposed carbohydrates like lipo- and exo-polysaccharides (EPS) is important for non-self recognition and responses to microbial associated molecular patterns in mammals and plants. In legumes, EPS are monitored and can either block or promote symbiosis with rhizobia depending on their molecular composition. To establish a deeper understanding of receptors involved in EPS recognition, we determined the structure of the Lotus japonicus (Lotus) exopolysaccharide receptor 3 (EPR3) ectodomain. EPR3 forms a compact structure built of three putative carbohydrate-binding modules (M1, M2 and LysM3). M1 and M2 have unique βαββ and βαβ folds that have not previously been observed in carbohydrate binding proteins, while LysM3 has a canonical βααβ fold. We demonstrate that this configuration is a structural signature for a ubiquitous class of receptors in the plant kingdom. We show that EPR3 is promiscuous, suggesting that plants can monitor complex microbial communities though this class of receptors.

Date: 2020
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DOI: 10.1038/s41467-020-17568-9

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