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The carbohydrate antigen dimeric Lewis X (DimLe x ), which accumulates in colonic and liver adenocarcinomas, is a valuable target to develop anti-cancer therapeutics. Using the native DimLe x antigen as a vaccine would elicit an autoimmune response against the Le x antigen found on normal, healthy cells. Thus, we aim to study the immunogenic potential of DimLe x and search internal epitopes displayed by DimLe x that remain to be recognized by anti-DimLe x monoclonal antibodies (mAbs) but no longer possess epitopes recognized by anti-Le x mAbs. In this context, we attempted to map the epitope recognized by anti-DimLe x mAb SH2 by titrations and competitive inhibition experiments using oligosaccharide fragments of DimLe x as well as Le x analogues. We compare our results with that reported for anti-Le x mAb SH1 and anti-polymeric Le x mAbs 1G5F6 and 291-2G3-A. While SH1 recognizes an epitope localized to the non-reducing end Le x trisaccharide, SH2, 1G5F6, and 291-2G3-A have greater affinity for DimLe x conjugates than for Le x conjugates. We show, however, that the Le x trisaccharide is still an important recognition element for SH2, which (like 1G5F6 and 291-2G3-A) makes contacts with all three sugar units of Le x . In contrast to mAb SH1, anti-polymeric Le x mAbs make contact with the Glc N Ac acetamido group, suggesting that epitopes extend further from the non-reducing end Le x . Results with SH2 show that this epitope is only recognized when DimLe x is presented by glycoconjugates. We have reported that DimLe x adopts two conformations around the β-d-Glc N Ac-(1→3)-d-Gal bond connecting the Le x trisaccharides. We propose that only one of these conformations is recognized by SH2 and that this conformation is favored when the hexasaccharide is presented as part of a glycoconjugate such as DimLe x -bovine serum albumin (DimLe x -BSA). Proper presentation of the oligosaccharide candidate via conjugation to a protein or lipid is essential for the design of an anti-cancer vaccine or immunotherapeutic based on DimLe x .

Recognition of Dimeric Lewis X by Anti-Dimeric Lex Antibody SH2