Sugar-Bind-ng Properties of the Two Lectin Domains of LEC-1 with Respect to the Gal beta 1-4Fuc Disaccharide Unit Present in Protostomia Glycoconjugates

摘要

Gal beta 1-4Fuc disaccharide unit was recently reported to be the endogenous structure recognized by the galectin LEC-6 isolated from the nematode Caenorhabditis elegans. LEC-1, which is another major galectin from this organism, is a tandem repeat-type galectin that contains two carbohydrate recognition domains, the N-terminal lectin domain (LEC-1Nh) and the C-terminal lectin domain (LEC-1Ch), and was also found to have an affinity for the Gal beta 1-4Fuc disaccharide unit. In the present study, we compared the binding strengths of LEC-1, LEC-1Nh, and LEC-1Ch to Gal beta 1-4Fuc, Gal beta 1-3Fuc, and Gal beta 1-4GIcNAc units as well as to LEC-6-ligand N-glycans by using frontal affinity chromatography (FAC) analysis. The two lectin domains of LEC-1 exhibited the highest affinity for Gal beta 1-4Fuc, though sugar-binding properties differed somewhat between LEC-1Nh and LEC-1Ch. Furthermore, these two domains had significantly lower affinities for the LEC-6-binding glycans. These results suggest that the endogenous recognition unit of LEC-1 is likely to be Gal beta 1-4Fuc, and that the endogenous ligands for LEC-1 are different from those for LEC-6.