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

TY - JOUR

T1 - Structural signatures in EPR3 define a unique class of plant carbohydrate receptors

AU - Wong, Jaslyn E.M.M.

AU - Gysel, Kira

AU - Birkefeldt, Thea G.

AU - Vinther, Maria

AU - Muszyński, Artur

AU - Azadi, Parastoo

AU - Laursen, Nick S.

AU - Sullivan, John T.

AU - Ronson, Clive W.

AU - Stougaard, Jens

AU - Andersen, Kasper R.

PY - 2020/7

Y1 - 2020/7

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85088830618&partnerID=8YFLogxK

U2 - 10.1038/s41467-020-17568-9

DO - 10.1038/s41467-020-17568-9

M3 - Journal article

C2 - 32732998

AN - SCOPUS:85088830618

SN - 2041-1723

VL - 11

JO - Nature Communications

JF - Nature Communications

M1 - 3797

ER -