Journal
PLOS PATHOGENS
Volume 6, Issue 1, Pages -Publisher
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.ppat.1000717
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Funding
- Swiss National Science Foundation [3100A3-116827, 200121101593]
- Roche Research Foundation
- European Molecular Biology Organization [ASTF-377.00-2008]
- Austrian Fonds zur Forderung der wissenschaftlichen Forschung [P18447, P20565]
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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 Gal beta 1,4Fuc alpha 1,6 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 Gal beta 1,4Fuc alpha 1,6GlcNAc trisaccharide at 1.5 angstrom 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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