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Structural signatures in EPR3 define a unique class of plant carbohydrate receptors
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 rh...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7392887/ https://www.ncbi.nlm.nih.gov/pubmed/32732998 http://dx.doi.org/10.1038/s41467-020-17568-9 |
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author | Wong, Jaslyn E. M. M. Gysel, Kira Birkefeldt, Thea G. Vinther, Maria Muszyński, Artur Azadi, Parastoo Laursen, Nick S. Sullivan, John T. Ronson, Clive W. Stougaard, Jens Andersen, Kasper R. |
author_facet | Wong, Jaslyn E. M. M. Gysel, Kira Birkefeldt, Thea G. Vinther, Maria Muszyński, Artur Azadi, Parastoo Laursen, Nick S. Sullivan, John T. Ronson, Clive W. Stougaard, Jens Andersen, Kasper R. |
author_sort | Wong, Jaslyn E. M. M. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-7392887 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-73928872020-08-12 Structural signatures in EPR3 define a unique class of plant carbohydrate receptors Wong, Jaslyn E. M. M. Gysel, Kira Birkefeldt, Thea G. Vinther, Maria Muszyński, Artur Azadi, Parastoo Laursen, Nick S. Sullivan, John T. Ronson, Clive W. Stougaard, Jens Andersen, Kasper R. Nat Commun Article 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. Nature Publishing Group UK 2020-07-30 /pmc/articles/PMC7392887/ /pubmed/32732998 http://dx.doi.org/10.1038/s41467-020-17568-9 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Wong, Jaslyn E. M. M. Gysel, Kira Birkefeldt, Thea G. Vinther, Maria Muszyński, Artur Azadi, Parastoo Laursen, Nick S. Sullivan, John T. Ronson, Clive W. Stougaard, Jens Andersen, Kasper R. Structural signatures in EPR3 define a unique class of plant carbohydrate receptors |
title | Structural signatures in EPR3 define a unique class of plant carbohydrate receptors |
title_full | Structural signatures in EPR3 define a unique class of plant carbohydrate receptors |
title_fullStr | Structural signatures in EPR3 define a unique class of plant carbohydrate receptors |
title_full_unstemmed | Structural signatures in EPR3 define a unique class of plant carbohydrate receptors |
title_short | Structural signatures in EPR3 define a unique class of plant carbohydrate receptors |
title_sort | structural signatures in epr3 define a unique class of plant carbohydrate receptors |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7392887/ https://www.ncbi.nlm.nih.gov/pubmed/32732998 http://dx.doi.org/10.1038/s41467-020-17568-9 |
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