Quick Search:

uzh logo
Browse by:
bullet
bullet
bullet
bullet

Zurich Open Repository and Archive 

Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-36731

Butschi, A; Titz, A; Wälti, M A; Olieric, V; Paschinger, K; Nöbauer, K; Guo, X; Seeberger, P H; Wilson, I B H; Aebi, M; Hengartner, M O; Künzler, M (2010). Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity towards nematotoxic fungal galectin CGL2. PLoS Pathogens, 6(1):e1000717.

[img]
Preview
PDF
2MB

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.

Item Type:Journal Article, refereed, original work
Communities & Collections:07 Faculty of Science > Institute of Molecular Life Sciences
DDC:570 Life sciences; biology
Language:English
Date:2010
Deposited On:05 Nov 2010 08:22
Last Modified:27 Nov 2013 18:57
Publisher:Public Library of Science
ISSN:1553-7366
Publisher DOI:10.1371/journal.ppat.1000717
PubMed ID:20062796
Citations:Web of Science®. Times Cited: 29
Google Scholar™
Scopus®. Citation Count: 31

Users (please log in): suggest update or correction for this item

Repository Staff Only: item control page