Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity towards nematotoxic fungal galectin CGL2.
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-b...
Guardado en:
| Autores principales: | , , , , , , , , , , , |
|---|---|
| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
Public Library of Science (PLoS)
2010
|
| Materias: | |
| Acceso en línea: | https://doaj.org/article/9436674aad2740f085e0ecbf4461a06c |
| Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
| id |
oai:doaj.org-article:9436674aad2740f085e0ecbf4461a06c |
|---|---|
| record_format |
dspace |
| spelling |
oai:doaj.org-article:9436674aad2740f085e0ecbf4461a06c2021-12-02T19:59:45ZCaenorhabditis elegans N-glycan core beta-galactoside confers sensitivity towards nematotoxic fungal galectin CGL2.1553-73661553-737410.1371/journal.ppat.1000717https://doaj.org/article/9436674aad2740f085e0ecbf4461a06c2010-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20062796/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374The 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.Alex ButschiAlexander TitzMartin A WältiVincent OliericKatharina PaschingerKatharina NöbauerXiaoqiang GuoPeter H SeebergerIain B H WilsonMarkus AebiMichael O HengartnerMarkus KünzlerPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 6, Iss 1, p e1000717 (2010) |
| institution |
DOAJ |
| collection |
DOAJ |
| language |
EN |
| topic |
Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 |
| spellingShingle |
Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Alex Butschi Alexander Titz Martin A Wälti Vincent Olieric Katharina Paschinger Katharina Nöbauer Xiaoqiang Guo Peter H Seeberger Iain B H Wilson Markus Aebi Michael O Hengartner Markus Künzler Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity towards nematotoxic fungal galectin CGL2. |
| description |
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. |
| format |
article |
| author |
Alex Butschi Alexander Titz Martin A Wälti Vincent Olieric Katharina Paschinger Katharina Nöbauer Xiaoqiang Guo Peter H Seeberger Iain B H Wilson Markus Aebi Michael O Hengartner Markus Künzler |
| author_facet |
Alex Butschi Alexander Titz Martin A Wälti Vincent Olieric Katharina Paschinger Katharina Nöbauer Xiaoqiang Guo Peter H Seeberger Iain B H Wilson Markus Aebi Michael O Hengartner Markus Künzler |
| author_sort |
Alex Butschi |
| title |
Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity towards nematotoxic fungal galectin CGL2. |
| title_short |
Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity towards nematotoxic fungal galectin CGL2. |
| title_full |
Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity towards nematotoxic fungal galectin CGL2. |
| title_fullStr |
Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity towards nematotoxic fungal galectin CGL2. |
| title_full_unstemmed |
Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity towards nematotoxic fungal galectin CGL2. |
| title_sort |
caenorhabditis elegans n-glycan core beta-galactoside confers sensitivity towards nematotoxic fungal galectin cgl2. |
| publisher |
Public Library of Science (PLoS) |
| publishDate |
2010 |
| url |
https://doaj.org/article/9436674aad2740f085e0ecbf4461a06c |
| work_keys_str_mv |
AT alexbutschi caenorhabditiselegansnglycancorebetagalactosideconferssensitivitytowardsnematotoxicfungalgalectincgl2 AT alexandertitz caenorhabditiselegansnglycancorebetagalactosideconferssensitivitytowardsnematotoxicfungalgalectincgl2 AT martinawalti caenorhabditiselegansnglycancorebetagalactosideconferssensitivitytowardsnematotoxicfungalgalectincgl2 AT vincentolieric caenorhabditiselegansnglycancorebetagalactosideconferssensitivitytowardsnematotoxicfungalgalectincgl2 AT katharinapaschinger caenorhabditiselegansnglycancorebetagalactosideconferssensitivitytowardsnematotoxicfungalgalectincgl2 AT katharinanobauer caenorhabditiselegansnglycancorebetagalactosideconferssensitivitytowardsnematotoxicfungalgalectincgl2 AT xiaoqiangguo caenorhabditiselegansnglycancorebetagalactosideconferssensitivitytowardsnematotoxicfungalgalectincgl2 AT peterhseeberger caenorhabditiselegansnglycancorebetagalactosideconferssensitivitytowardsnematotoxicfungalgalectincgl2 AT iainbhwilson caenorhabditiselegansnglycancorebetagalactosideconferssensitivitytowardsnematotoxicfungalgalectincgl2 AT markusaebi caenorhabditiselegansnglycancorebetagalactosideconferssensitivitytowardsnematotoxicfungalgalectincgl2 AT michaelohengartner caenorhabditiselegansnglycancorebetagalactosideconferssensitivitytowardsnematotoxicfungalgalectincgl2 AT markuskunzler caenorhabditiselegansnglycancorebetagalactosideconferssensitivitytowardsnematotoxicfungalgalectincgl2 |
| _version_ |
1718375738095173632 |