The ISOBM TD-4 Workshop antibodies 122–177 were grouped according to their reactivity with: (a) monomeric MUC1 peptide (TAP25); (b) the pentameric tandem repeat peptide (TR-5), both unglycosylated or as their GalNAc-substituted derivatives, and (c) the lactation or tumor-associated glycoforms of MUC1. The antibodies were grouped into nine clusters: Clusters 1–4 comprise those antibodies that bind to MUC1 tandem repeat peptide (monomeric) and define sequential epitopes differentially affected by glycosylation (GalNAc substitution) in the peptide motifs VTSA and GSTA. The ISOBM-163 antibody in cluster 5 defines Tn antigen as a site-specific glycotope within the tandem repeat peptide. The antibodies in clusters 6 and 7A recognize peptide epitopes within the tandem repeats, although these seem to be conformationally dependent on complex glycosylation or on oligomeric peptide repetition. Antibodies in clusters 7B bind to a conformational epitope not related to the tandem repeat peptide or to a carbohydrate epitope (cluster 7BC). Antibodies in cluster 8 showed a high selective binding to tumor-associated epitopes on MUC1 from mammary carcinoma cells. Cluster 9 antibodies were not reactive on any of the tested antigens and may be argued to lack MUC1 specificity. Alternatively, these antibodies could have a carbohydrate specificity not expressed by the MUC1 glycoforms tested in our studies.

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