PubMed:19690090 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/19690090","sourcedb":"PubMed","sourceid":"19690090","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/19690090","text":"Caenorhabditis elegans galectins LEC-6 and LEC-1 recognize a chemically synthesized Galbeta1-4Fuc disaccharide unit which is present in Protostomia glycoconjugates.\nGalbeta1-4GlcNAc is thought to be a common disaccharide unit preferentially recognized by vertebrate galectins. Eight-amino-acid residues conserved in proteins belonging to the galectin family have been suggested to be responsible for recognition. Meanwhile, we isolated and analyzed endogenous N-glycans of Caenorhabditis elegans that were captured by a C. elegans galectin LEC-6 and demonstrated that the unit of recognition for LEC-6 is a Gal-Fuc disaccharide, though the linkage between these residues was not confirmed. In the present study, we chemically synthesized Galbeta1-4Fuc and Galbeta1-3Fuc labeled with 2-aminopyridine (PA) and demonstrated that LEC-6 interacts with PA-Galbeta1-4Fuc more strongly than PA-Galbeta1-3Fuc by frontal affinity chromatography (FAC). Galbeta1-4Fuc also inhibited hemagglutination caused by LEC-6 more strongly than Galbeta1-3Fuc. FAC analysis using LEC-6 point mutants revealed that some of the conserved amino acid residues which have proven to be important for the recognition of Galbeta1-4GlcNAc are not necessary for the binding to Galbeta1-4Fuc. Another major C. elegans galectin, LEC-1, also showed preferential binding to Galbeta1-4Fuc. These results suggest that Galbeta1-4Fuc is the endogenous unit structure recognized by C. elegans galectins, which implies that C. elegans glycans and galectins may have co-evolved through an alteration in the structures of C. elegans glycans and a subsequent conversion in the sugar-binding mechanism of galectins. Furthermore, since glycans containing the Galbeta1-4Fuc disaccharide unit have been found in organisms belonging to Protostomia, this unit might be a common glyco-epitope recognized by galectins in these 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