Mapping the Epitopes Recognized by Monoclonal Anti-Lewis X and Anti-Lewis A Antibodies
Aberrant glycosylation is a common biochemical phenomenon associated with cancer. The aberrations in glycan structure, referred to as Tumor Associated Carbohydrate Antigens (TACAs), offer a promising avenue for targeted cancer immunotherapy, specifically for the design of epitope-based vaccines. The primary goal of designing such vaccines is to be able to target these antigens while avoiding an autoimmune response. Therefore, the understanding of the immunogenic potential of the specific antigen is critical in the development of TACA-based vaccines. Epitope mapping of monoclonal antibodies (mAbs) is a widely used technique in evaluating the immunogenic potential of such target antigens. Two TACAs of particular interest to our research group are the dimeric Lewis X (dimLex) and Lewis A Lewis X (LeaLex) hexasaccharides. Herein, we describe the characterization of three anti-TACA mAbs: IG5F6, SH2 and SPM 522. The work presented here provides valuable insight into identifying promising TACA-based therapeutic targets.