2.50
Hdl Handle:
http://hdl.handle.net/10033/326069
Title:
Methylated glycans as conserved targets of animal and fungal innate defense.
Authors:
Wohlschlager, Therese; Butschi, Alex; Grassi, Paola; Sutov, Grigorij; Gauss, Robert; Hauck, Dirk; Schmieder, Stefanie S; Knobel, Martin; Titz, Alexander; Dell, Anne; Haslam, Stuart M; Hengartner, Michael O; Aebi, Markus; Künzler, Markus
Abstract:
Effector proteins of innate immune systems recognize specific non-self epitopes. Tectonins are a family of β-propeller lectins conserved from bacteria to mammals that have been shown to bind bacterial lipopolysaccharide (LPS). We present experimental evidence that two Tectonins of fungal and animal origin have a specificity for O-methylated glycans. We show that Tectonin 2 of the mushroom Laccaria bicolor (Lb-Tec2) agglutinates Gram-negative bacteria and exerts toxicity toward the model nematode Caenorhabditis elegans, suggesting a role in fungal defense against bacteria and nematodes. Biochemical and genetic analysis of these interactions revealed that both bacterial agglutination and nematotoxicity of Lb-Tec2 depend on the recognition of methylated glycans, namely O-methylated mannose and fucose residues, as part of bacterial LPS and nematode cell-surface glycans. In addition, a C. elegans gene, termed samt-1, coding for a candidate membrane transport protein for the presumptive donor substrate of glycan methylation, S-adenosyl-methionine, from the cytoplasm to the Golgi was identified. Intriguingly, limulus lectin L6, a structurally related antibacterial protein of the Japanese horseshoe crab Tachypleus tridentatus, showed properties identical to the mushroom lectin. These results suggest that O-methylated glycans constitute a conserved target of the fungal and animal innate immune system. The broad phylogenetic distribution of O-methylated glycans increases the spectrum of potential antagonists recognized by Tectonins, rendering this conserved protein family a universal defense armor.
Citation:
Methylated glycans as conserved targets of animal and fungal innate defense. 2014, 111 (27):E2787-96 Proc. Natl. Acad. Sci. U.S.A.
Journal:
Proceedings of the National Academy of Sciences of the United States of America
Issue Date:
8-Jul-2014
URI:
http://hdl.handle.net/10033/326069
DOI:
10.1073/pnas.1401176111
PubMed ID:
24879441
Type:
Article
Language:
en
ISSN:
1091-6490
Appears in Collections:
publications of the junior research group chemical biology of carbohydrates ([HIPS]CBCH)

Full metadata record

DC FieldValue Language
dc.contributor.authorWohlschlager, Thereseen
dc.contributor.authorButschi, Alexen
dc.contributor.authorGrassi, Paolaen
dc.contributor.authorSutov, Grigorijen
dc.contributor.authorGauss, Roberten
dc.contributor.authorHauck, Dirken
dc.contributor.authorSchmieder, Stefanie Sen
dc.contributor.authorKnobel, Martinen
dc.contributor.authorTitz, Alexanderen
dc.contributor.authorDell, Anneen
dc.contributor.authorHaslam, Stuart Men
dc.contributor.authorHengartner, Michael Oen
dc.contributor.authorAebi, Markusen
dc.contributor.authorKünzler, Markusen
dc.date.accessioned2014-09-12T09:43:18Z-
dc.date.available2014-09-12T09:43:18Z-
dc.date.issued2014-07-08-
dc.identifier.citationMethylated glycans as conserved targets of animal and fungal innate defense. 2014, 111 (27):E2787-96 Proc. Natl. Acad. Sci. U.S.A.en
dc.identifier.issn1091-6490-
dc.identifier.pmid24879441-
dc.identifier.doi10.1073/pnas.1401176111-
dc.identifier.urihttp://hdl.handle.net/10033/326069-
dc.description.abstractEffector proteins of innate immune systems recognize specific non-self epitopes. Tectonins are a family of β-propeller lectins conserved from bacteria to mammals that have been shown to bind bacterial lipopolysaccharide (LPS). We present experimental evidence that two Tectonins of fungal and animal origin have a specificity for O-methylated glycans. We show that Tectonin 2 of the mushroom Laccaria bicolor (Lb-Tec2) agglutinates Gram-negative bacteria and exerts toxicity toward the model nematode Caenorhabditis elegans, suggesting a role in fungal defense against bacteria and nematodes. Biochemical and genetic analysis of these interactions revealed that both bacterial agglutination and nematotoxicity of Lb-Tec2 depend on the recognition of methylated glycans, namely O-methylated mannose and fucose residues, as part of bacterial LPS and nematode cell-surface glycans. In addition, a C. elegans gene, termed samt-1, coding for a candidate membrane transport protein for the presumptive donor substrate of glycan methylation, S-adenosyl-methionine, from the cytoplasm to the Golgi was identified. Intriguingly, limulus lectin L6, a structurally related antibacterial protein of the Japanese horseshoe crab Tachypleus tridentatus, showed properties identical to the mushroom lectin. These results suggest that O-methylated glycans constitute a conserved target of the fungal and animal innate immune system. The broad phylogenetic distribution of O-methylated glycans increases the spectrum of potential antagonists recognized by Tectonins, rendering this conserved protein family a universal defense armor.en
dc.language.isoenen
dc.rightsArchived with thanks to Proceedings of the National Academy of Sciences of the United States of Americaen
dc.titleMethylated glycans as conserved targets of animal and fungal innate defense.en
dc.typeArticleen
dc.identifier.journalProceedings of the National Academy of Sciences of the United States of Americaen

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