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Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity towards nematotoxic fungal galectin CGL2.
Butschi, Alex Titz, Alexander Wälti, Martin A Olieric, Vincent Paschinger, Katharina Nöbauer, Katharina Guo, Xiaoqiang Seeberger, Peter H Wilson, Iain B H Aebi, Markus
Butschi, Alex
Titz, Alexander
Wälti, Martin A
Olieric, Vincent
Paschinger, Katharina
Nöbauer, Katharina
Guo, Xiaoqiang
Seeberger, Peter H
Wilson, Iain B H
Aebi, Markus
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2010-01
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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.
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Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity towards nematotoxic fungal galectin CGL2. 2010, 6 (1):e1000717 PLoS Pathog.
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en
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1553-7374