Oligosaccharide structural specificity of the soluble agglutinin released from guinea pig colonic epithelial cells

Abstract

Guinea pig colonic epithelial cells release a soluble lectin capable of agglutinating numerous strains of Shigella and Escherichia coli as well as other bacteria. Using pure oligosaccharides and glycopeptides with well-defined structures to inhibit the agglutination of Shigella flexneri 1b by the soluble intestinal lectin, we have been able to demonstrate that the latter recognises different structural types. Inhibition by human milk glucoprotein glycopeptides with biantennary glycans of the N-acetyllactosamine type was dependent on the simultaneous presence of unsubstituted terminal non-reducing galactose residues and of a fucose residue α-1,6-linked to the asparagine-conjugated N-acetylglucosamine residue. Unsubstituted terminal non-reducing galactose was also determinant for inhibition by human milk oligosaccharides. Finally oligosaccharides possessing the Man (α1–2) Man structure inhibited more effectively than those with a Man(α1–3)Man sequence. The fact that these different structural motifs were all inhibitory raises the problem of the possible existence of a multispecific lectin or of several different lectins in the guinea pig colonic mucosa mediating bacterial adherence.