Galectin-2 suppresses nematode development by binding to the invertebrate-specific galactoseβ1-4fucose glyco-epitope. (23rd April 2019)
- Record Type:
- Journal Article
- Title:
- Galectin-2 suppresses nematode development by binding to the invertebrate-specific galactoseβ1-4fucose glyco-epitope. (23rd April 2019)
- Main Title:
- Galectin-2 suppresses nematode development by binding to the invertebrate-specific galactoseβ1-4fucose glyco-epitope
- Authors:
- Takeuchi, Tomoharu
Tamura, Mayumi
Ishiwata, Kenji
Hamasaki, Megumi
Hamano, Shinjiro
Arata, Yoichiro
Hatanaka, Tomomi - Abstract:
- Abstract: Galactoseβ1-4Fucose (GalFuc) is a unique disaccharide found in invertebrates including nematodes. A fungal galectin CGL2 suppresses nematode development by recognizing the galactoseβ1-4fucose epitope. The Caenorhabditis elegans galectin LEC-6 recognizes it as an endogenous ligand and the Glu 67 residue of LEC-6 is responsible for this interaction. We found that mammalian galectin-2 (Gal-2) also has a comparable glutamate residue, Glu 52 . In the present study, we investigated the potential nematode-suppressing activity of Gal-2 using C. elegans as a model and focusing on Gal-2 binding to the GalFuc epitope. Gal-2 suppressed C. elegans development whereas its E52D mutant (Glu 52 substituted by Asp), galectin-1 and galectin-3 had little effect on C. elegans growth. Lectin-staining using fluorescently-labeled Gal-2 revealed that, like CGL2, it specifically binds to the C. elegans intestine. Natural C. elegans glycoconjugates were specifically bound by immobilized Gal-2. Western blotting with anti-GalFuc antibody showed that the bound glycoconjugates had the GalFuc epitope. Frontal affinity chromatography with pyridylamine-labeled C. elegans N -glycans disclosed that Gal-2 (but not its E52D mutant) recognizes the GalFuc epitope. Gal-2 also binds to the GalFuc-bearing glycoconjugates of Ascaris and the GalFuc epitope is present in the parasitic nematodes Nippostrongylus brasiliensis and Brugia pahangi . These results indicate that Gal-2 suppresses C. elegans developmentAbstract: Galactoseβ1-4Fucose (GalFuc) is a unique disaccharide found in invertebrates including nematodes. A fungal galectin CGL2 suppresses nematode development by recognizing the galactoseβ1-4fucose epitope. The Caenorhabditis elegans galectin LEC-6 recognizes it as an endogenous ligand and the Glu 67 residue of LEC-6 is responsible for this interaction. We found that mammalian galectin-2 (Gal-2) also has a comparable glutamate residue, Glu 52 . In the present study, we investigated the potential nematode-suppressing activity of Gal-2 using C. elegans as a model and focusing on Gal-2 binding to the GalFuc epitope. Gal-2 suppressed C. elegans development whereas its E52D mutant (Glu 52 substituted by Asp), galectin-1 and galectin-3 had little effect on C. elegans growth. Lectin-staining using fluorescently-labeled Gal-2 revealed that, like CGL2, it specifically binds to the C. elegans intestine. Natural C. elegans glycoconjugates were specifically bound by immobilized Gal-2. Western blotting with anti-GalFuc antibody showed that the bound glycoconjugates had the GalFuc epitope. Frontal affinity chromatography with pyridylamine-labeled C. elegans N -glycans disclosed that Gal-2 (but not its E52D mutant) recognizes the GalFuc epitope. Gal-2 also binds to the GalFuc-bearing glycoconjugates of Ascaris and the GalFuc epitope is present in the parasitic nematodes Nippostrongylus brasiliensis and Brugia pahangi . These results indicate that Gal-2 suppresses C. elegans development by binding to its GalFuc epitope. The findings also imply that Gal-2 may prevent infestations of various parasitic nematodes bearing the GalFuc epitope. … (more)
- Is Part Of:
- Glycobiology. Volume 29:Number 6(2019)
- Journal:
- Glycobiology
- Issue:
- Volume 29:Number 6(2019)
- Issue Display:
- Volume 29, Issue 6 (2019)
- Year:
- 2019
- Volume:
- 29
- Issue:
- 6
- Issue Sort Value:
- 2019-0029-0006-0000
- Page Start:
- 504
- Page End:
- 512
- Publication Date:
- 2019-04-23
- Subjects:
- Caenorhabditis elegans -- galactoseβ1-4fucose -- galectin -- nematode -- parasite
Glycoproteins -- Periodicals
Glycolipids -- Periodicals
Glycoconjugates -- Periodicals
572.567 - Journal URLs:
- http://glycob.oupjournals.org/ ↗
http://ukcatalogue.oup.com/ ↗ - DOI:
- 10.1093/glycob/cwz022 ↗
- Languages:
- English
- ISSNs:
- 0959-6658
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4196.303000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 11778.xml