Abstract
The molecular basis of antibody 5E5, which recognizes the entire GalNAc unit as a primary epitope is disclosed. The antibody's contacts with the peptide are mostly limited to two residues, allowing it to show some degree of promiscuity. These findings open the door to the chemical design of peptide-mimetics for developing efficient anti-cancer vaccines and diagnostic tools.
Highlights
The molecular basis of antibody 5E5, which recognizes the entire GalNAc unit as a primary epitope is disclosed
The antibody's contacts with the peptide are limited to mostly two residues, allowing it to show some degree of promiscuity
MUC1 exhibits complex O-glycans in healthy cells, in tumour tissues it is decorated with short carbohydrates
Summary
Structural Characterization of an Unprecedented Lectin-like Antitumoral anti-MUC1 Antibody. Despite the vast amount of clinical and immunological data available on antibodies that recognize aberrantly glycosylated MUC1, the molecular details by which these antibodies recognize their targets are scarce.6 This structural knowledge is fundamental to the development of new anti-MUC1 antibodies with improved specificities to advance cancer therapy.. From a molecular recognition perspective, most of anti-MUC1 monoclonal antibodies (mAb) recognize the peptide sequence DTRP, recent studies indicate that some bind to GSTAP or GVTS motifs.. Binding is enhanced by glycosylation of the PDTR epitope In this respect, the X-ray structure of the complex between antibody AR20.5 and glycopeptide APDT*RP (in which T* = Tn-Thr = GalNAc-D-1-O-Thr) reveals that the contacts between the sugar and the antibody are negligible.. We could not determine any binding of the antibody against GalNAc-D-1-O-Me, probably due to the very low affinity, as previously reported. the presence of two Tn antigens in the peptide (glycopeptide 3)
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