Crystal Structures of Fungal Tectonin in Complex with O-Methylated Glycans Suggest Key Role in Innate Immune Defense.
dc.contributor.author | Sommer, Roman | |
dc.contributor.author | Makshakova, Olga N | |
dc.contributor.author | Wohlschlager, Therese | |
dc.contributor.author | Hutin, Stephanie | |
dc.contributor.author | Marsh, May | |
dc.contributor.author | Titz, Alexander | |
dc.contributor.author | Künzler, Markus | |
dc.contributor.author | Varrot, Annabelle | |
dc.date.accessioned | 2018-05-07T12:38:06Z | |
dc.date.available | 2018-05-07T12:38:06Z | |
dc.date.issued | 2018-03-06 | |
dc.identifier.citation | Crystal Structures of Fungal Tectonin in Complex with O-Methylated Glycans Suggest Key Role in Innate Immune Defense. 2018, 26 (3):391-402.e4 Structure | en |
dc.identifier.issn | 1878-4186 | |
dc.identifier.pmid | 29398527 | |
dc.identifier.doi | 10.1016/j.str.2018.01.003 | |
dc.identifier.uri | http://hdl.handle.net/10033/621366 | |
dc.description.abstract | Innate immunity is the first line of defense against pathogens and predators. To initiate a response, it relies on the detection of invaders, where lectin-carbohydrate interactions play a major role. O-Methylated glycans were previously identified as non-self epitopes and conserved targets for defense effector proteins belonging to the tectonin superfamily. Here, we present two crystal structures of Tectonin 2 from the mushroom Laccaria bicolor in complex with methylated ligands, unraveling the molecular basis for this original specificity. Furthermore, they revealed the formation of a ball-shaped tetramer with 24 binding sites distributed at its surface, resembling a small virus capsid. Based on the crystal structures, a methylation recognition motif was identified and found in the sequence of many tectonins from bacteria to human. Our results support a key role of tectonins in innate defense based on a distinctive and conserved type of lectin-glycan interaction. | |
dc.language.iso | en | en |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-sa/4.0/ | * |
dc.title | Crystal Structures of Fungal Tectonin in Complex with O-Methylated Glycans Suggest Key Role in Innate Immune Defense. | en |
dc.type | Article | en |
dc.contributor.department | HIPS, Helmholtz-Institut für pharmazeutische Forschung Saarland, Universitätscampus 8.1, 66123 Saarbrücken, Germany. | en |
dc.identifier.journal | Structure (London, England : 1993) | en |
refterms.dateFOA | 2019-03-15T00:00:00Z | |
html.description.abstract | Innate immunity is the first line of defense against pathogens and predators. To initiate a response, it relies on the detection of invaders, where lectin-carbohydrate interactions play a major role. O-Methylated glycans were previously identified as non-self epitopes and conserved targets for defense effector proteins belonging to the tectonin superfamily. Here, we present two crystal structures of Tectonin 2 from the mushroom Laccaria bicolor in complex with methylated ligands, unraveling the molecular basis for this original specificity. Furthermore, they revealed the formation of a ball-shaped tetramer with 24 binding sites distributed at its surface, resembling a small virus capsid. Based on the crystal structures, a methylation recognition motif was identified and found in the sequence of many tectonins from bacteria to human. Our results support a key role of tectonins in innate defense based on a distinctive and conserved type of lectin-glycan interaction. |