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dc.contributor.authorSommer, Roman
dc.contributor.authorMakshakova, Olga N
dc.contributor.authorWohlschlager, Therese
dc.contributor.authorHutin, Stephanie
dc.contributor.authorMarsh, May
dc.contributor.authorTitz, Alexander
dc.contributor.authorKünzler, Markus
dc.contributor.authorVarrot, Annabelle
dc.date.accessioned2018-05-07T12:38:06Z
dc.date.available2018-05-07T12:38:06Z
dc.date.issued2018-03-06
dc.identifier.citationCrystal Structures of Fungal Tectonin in Complex with O-Methylated Glycans Suggest Key Role in Innate Immune Defense. 2018, 26 (3):391-402.e4 Structureen
dc.identifier.issn1878-4186
dc.identifier.pmid29398527
dc.identifier.doi10.1016/j.str.2018.01.003
dc.identifier.urihttp://hdl.handle.net/10033/621366
dc.description.abstractInnate 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.isoenen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.titleCrystal Structures of Fungal Tectonin in Complex with O-Methylated Glycans Suggest Key Role in Innate Immune Defense.en
dc.typeArticleen
dc.contributor.departmentHIPS, Helmholtz-Institut für pharmazeutische Forschung Saarland, Universitätscampus 8.1, 66123 Saarbrücken, Germany.en
dc.identifier.journalStructure (London, England : 1993)en
refterms.dateFOA2019-03-15T00:00:00Z
html.description.abstractInnate 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.


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