2.50
Hdl Handle:
http://hdl.handle.net/10033/336553
Title:
Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity towards nematotoxic fungal galectin CGL2.
Authors:
Butschi, Alex; Titz, Alexander; Wälti, Martin A; Olieric, Vincent; Paschinger, Katharina; Nöbauer, Katharina; Guo, Xiaoqiang; Seeberger, Peter H; Wilson, Iain B H; Aebi, Markus; Hengartner, Michael O; Künzler, Markus
Abstract:
The physiological role of fungal galectins has remained elusive. Here, we show that feeding of a mushroom galectin, Coprinopsis cinerea CGL2, to Caenorhabditis elegans inhibited development and reproduction and ultimately resulted in killing of this nematode. The lack of toxicity of a carbohydrate-binding defective CGL2 variant and the resistance of a C. elegans mutant defective in GDP-fucose biosynthesis suggested that CGL2-mediated nematotoxicity depends on the interaction between the galectin and a fucose-containing glycoconjugate. A screen for CGL2-resistant worm mutants identified this glycoconjugate as a Galbeta1,4Fucalpha1,6 modification of C. elegans N-glycan cores. Analysis of N-glycan structures in wild type and CGL2-resistant nematodes confirmed this finding and allowed the identification of a novel putative glycosyltransferase required for the biosynthesis of this glycoepitope. The X-ray crystal structure of a complex between CGL2 and the Galbeta1,4Fucalpha1,6GlcNAc trisaccharide at 1.5 A resolution revealed the biophysical basis for this interaction. Our results suggest that fungal galectins play a role in the defense of fungi against predators by binding to specific glycoconjugates of these organisms.
Affiliation:
Institute of Molecular Biology, University of Zürich, Zürich, Switzerland.
Citation:
Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity towards nematotoxic fungal galectin CGL2. 2010, 6 (1):e1000717 PLoS Pathog.
Journal:
PLoS pathogens
Issue Date:
Jan-2010
URI:
http://hdl.handle.net/10033/336553
DOI:
10.1371/journal.ppat.1000717
PubMed ID:
20062796
Type:
Article
Language:
en
ISSN:
1553-7374
Appears in Collections:
publications of the junior research group chemical biology of carbohydrates ([HIPS]CBCH)

Full metadata record

DC FieldValue Language
dc.contributor.authorButschi, Alexen
dc.contributor.authorTitz, Alexanderen
dc.contributor.authorWälti, Martin Aen
dc.contributor.authorOlieric, Vincenten
dc.contributor.authorPaschinger, Katharinaen
dc.contributor.authorNöbauer, Katharinaen
dc.contributor.authorGuo, Xiaoqiangen
dc.contributor.authorSeeberger, Peter Hen
dc.contributor.authorWilson, Iain B Hen
dc.contributor.authorAebi, Markusen
dc.contributor.authorHengartner, Michael Oen
dc.contributor.authorKünzler, Markusen
dc.date.accessioned2014-12-03T10:32:51Z-
dc.date.available2014-12-03T10:32:51Z-
dc.date.issued2010-01-
dc.identifier.citationCaenorhabditis elegans N-glycan core beta-galactoside confers sensitivity towards nematotoxic fungal galectin CGL2. 2010, 6 (1):e1000717 PLoS Pathog.en
dc.identifier.issn1553-7374-
dc.identifier.pmid20062796-
dc.identifier.doi10.1371/journal.ppat.1000717-
dc.identifier.urihttp://hdl.handle.net/10033/336553-
dc.description.abstractThe physiological role of fungal galectins has remained elusive. Here, we show that feeding of a mushroom galectin, Coprinopsis cinerea CGL2, to Caenorhabditis elegans inhibited development and reproduction and ultimately resulted in killing of this nematode. The lack of toxicity of a carbohydrate-binding defective CGL2 variant and the resistance of a C. elegans mutant defective in GDP-fucose biosynthesis suggested that CGL2-mediated nematotoxicity depends on the interaction between the galectin and a fucose-containing glycoconjugate. A screen for CGL2-resistant worm mutants identified this glycoconjugate as a Galbeta1,4Fucalpha1,6 modification of C. elegans N-glycan cores. Analysis of N-glycan structures in wild type and CGL2-resistant nematodes confirmed this finding and allowed the identification of a novel putative glycosyltransferase required for the biosynthesis of this glycoepitope. The X-ray crystal structure of a complex between CGL2 and the Galbeta1,4Fucalpha1,6GlcNAc trisaccharide at 1.5 A resolution revealed the biophysical basis for this interaction. Our results suggest that fungal galectins play a role in the defense of fungi against predators by binding to specific glycoconjugates of these organisms.en
dc.language.isoenen
dc.subject.meshAgaricalesen
dc.subject.meshAmino Acid Sequenceen
dc.subject.meshAnimalsen
dc.subject.meshCaenorhabditis elegansen
dc.subject.meshCaenorhabditis elegans Proteinsen
dc.subject.meshFungal Proteinsen
dc.subject.meshGalactosidesen
dc.subject.meshGalectin 2en
dc.subject.meshMolecular Sequence Dataen
dc.subject.meshNematode Infectionsen
dc.subject.meshProtein Structure, Quaternaryen
dc.subject.meshStructure-Activity Relationshipen
dc.titleCaenorhabditis elegans N-glycan core beta-galactoside confers sensitivity towards nematotoxic fungal galectin CGL2.en
dc.typeArticleen
dc.contributor.departmentInstitute of Molecular Biology, University of Zürich, Zürich, Switzerland.en
dc.identifier.journalPLoS pathogensen

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