Novel carbohydrate specificity of monoclonal antibody 91.9H prepared against human colonic sulfomucin: recognition of sulfo-Lewis(a) structure.

Monoclonal antibody (mAb) 91.9H was previously prepared against partially purified human colonic sulfomucins. The epitope was detected in normal colonic mucosa and primary and metastatic colorectal carcinoma in decreasing order of magnitude. In the present study, this antibody was shown to recognize sulfo-Le(a) structure, HSO3-3Gal beta 1-3(Fuc alpha 1-4)GlcNAc. Interactions between mAb 91.9H and synthetic oligosaccharides conjugated with biotinylated polyacrylamide carrier were examined by a biosensor based on surface plasmon resonance and by enzyme-linked immunosorbent assays. This mAb bound to sulfo-Lea but not to sulfo-LeX, Le(a), LeX, sialyl-Le(a), or sialyl-LeX. Sulfo-Le(a) oligosaccharides decreased its binding affinity with mAb 91.9H after periodate oxidation of its fucose residue. Immunohistochemical study showed a strong binding of mAb 91.9H to goblet cells in human colonic epithelia of Lewis-positive individuals but a trace binding in Lewis-negative individuals, confirming the specificity of this antibody toward structures containing a fucosylated type 1 backbone. Copyright 1998 Academic Press.