Immobilized Lotus tetragonolobus agglutinin binds oligosaccharides containing the Le(x) determinant.

A defined set of oligosaccharides and glycopeptides containing alpha-linked fucose were used to examine the specificity of the immobilized fucose-binding lectin Lotus tetragonolobus agglutinin (LTA1), also known as lotus lectin. Glycans containing the Lewis x determinant (Le(x)) Gal beta 1-4[Fuc alpha 1-3]GlcNAc beta 1-3-R were significantly retarded in elution from high density LTA-Emphaze columns. The lectin also bound the fucosylated lacdiNAc trisaccharide GalNAc beta 1-4[Fuc alpha 1-3]GlcNAc. The lectin did not bind glycans containing either sialylLe(x) or VIM-2 determinants, nor did it bind the isomeric Le(x), Gal beta 1-3[Fuc alpha 1-4]GlcNAc-R. Although 2'-fucosyllactose Fuc alpha 1-2Gal beta 1-4Glc) was retarded in elution from the columns, larger glycans containing the H-antigen Fuc alpha 1-2Gal beta 1-3(4)GlcNAc-R interacted poorly with immobilized LTA. Our results demonstrate that immobilized LTA is effective in isolating glycans containing the Le(x) antigen and is useful in analyzing specific fucosylation of glycoconjugates.