Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity towards nematotoxic fungal galectin CGL2.
Butschi et al_final.pdf
Open Access publication
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
Wälti, Martin A
Seeberger, Peter H
Wilson, Iain B H
Hengartner, Michael O
MetadataShow full item record
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.
CitationCaenorhabditis elegans N-glycan core beta-galactoside confers sensitivity towards nematotoxic fungal galectin CGL2. 2010, 6 (1):e1000717 PLoS Pathog.
AffiliationInstitute of Molecular Biology, University of Zürich, Zürich, Switzerland.
The following license files are associated with this item:
- Plasticity of the β-trefoil protein fold in the recognition and control of invertebrate predators and parasites by a fungal defence system.
- Authors: Schubert M, Bleuler-Martinez S, Butschi A, Wälti MA, Egloff P, Stutz K, Yan S, Collot M, Mallet JM, Wilson IB, Hengartner MO, Aebi M, Allain FH, Künzler M
- Issue date: 2012
- Galactosylated fucose epitopes in nematodes: increased expression in a Caenorhabditis mutant associated with altered lectin sensitivity and occurrence in parasitic species.
- Authors: Yan S, Bleuler-Martinez S, Plaza DF, Künzler M, Aebi M, Joachim A, Razzazi-Fazeli E, Jantsch V, Geyer R, Wilson IB, Paschinger K
- Issue date: 2012 Aug 17
- Galactoseβ1-4fucose: A unique disaccharide unit found in N-glycans of invertebrates including nematodes.
- Authors: Takeuchi T, Arata Y, Kasai KI
- Issue date: 2016 Dec
- Structure and functional analysis of the fungal galectin CGL2.
- Authors: Walser PJ, Haebel PW, Künzler M, Sargent D, Kües U, Aebi M, Ban N
- Issue date: 2004 Apr
- Molecular basis for galactosylation of core fucose residues in invertebrates: identification of caenorhabditis elegans N-glycan core alpha1,6-fucoside beta1,4-galactosyltransferase GALT-1 as a member of a novel glycosyltransferase family.
- Authors: Titz A, Butschi A, Henrissat B, Fan YY, Hennet T, Razzazi-Fazeli E, Hengartner MO, Wilson IBH, Künzler M, Aebi M
- Issue date: 2009 Dec 25