Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity towards nematotoxic fungal galectin CGL2.
dc.contributor.author | Butschi, Alex | |
dc.contributor.author | Titz, Alexander | |
dc.contributor.author | Wälti, Martin A | |
dc.contributor.author | Olieric, Vincent | |
dc.contributor.author | Paschinger, Katharina | |
dc.contributor.author | Nöbauer, Katharina | |
dc.contributor.author | Guo, Xiaoqiang | |
dc.contributor.author | Seeberger, Peter H | |
dc.contributor.author | Wilson, Iain B H | |
dc.contributor.author | Aebi, Markus | |
dc.contributor.author | Hengartner, Michael O | |
dc.contributor.author | Künzler, Markus | |
dc.date.accessioned | 2014-12-03T10:32:51Z | |
dc.date.available | 2014-12-03T10:32:51Z | |
dc.date.issued | 2010-01 | |
dc.identifier.citation | Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity towards nematotoxic fungal galectin CGL2. 2010, 6 (1):e1000717 PLoS Pathog. | en |
dc.identifier.issn | 1553-7374 | |
dc.identifier.pmid | 20062796 | |
dc.identifier.doi | 10.1371/journal.ppat.1000717 | |
dc.identifier.uri | http://hdl.handle.net/10033/336553 | |
dc.description.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. | |
dc.language.iso | en | en |
dc.subject.mesh | Agaricales | en |
dc.subject.mesh | Amino Acid Sequence | en |
dc.subject.mesh | Animals | en |
dc.subject.mesh | Caenorhabditis elegans | en |
dc.subject.mesh | Caenorhabditis elegans Proteins | en |
dc.subject.mesh | Fungal Proteins | en |
dc.subject.mesh | Galactosides | en |
dc.subject.mesh | Galectin 2 | en |
dc.subject.mesh | Molecular Sequence Data | en |
dc.subject.mesh | Nematode Infections | en |
dc.subject.mesh | Protein Structure, Quaternary | en |
dc.subject.mesh | Structure-Activity Relationship | en |
dc.title | Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity towards nematotoxic fungal galectin CGL2. | en |
dc.type | Article | en |
dc.contributor.department | Institute of Molecular Biology, University of Zürich, Zürich, Switzerland. | en |
dc.identifier.journal | PLoS pathogens | en |
refterms.dateFOA | 2018-06-13T03:47:23Z | |
html.description.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. |