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Summary report on the ISOBM TD-4 Workshop: analysis of 56 monoclonal antibodies against the MUC1 mucin

Item Type:Article
Title:Summary report on the ISOBM TD-4 Workshop: analysis of 56 monoclonal antibodies against the MUC1 mucin
Creators Name:Price, M. and Rye, P. and Petrakou, E. and Murray, A. and Brady, K. and Imai, S. and Haga, S. and Kiyozuka, Y. and Schol, D. and Meulenbroek, M. and Snijdewint, F. and von Mensdorff-Pouilly, S. and Verstraeten, R. and Kenemans, P. and Blockzjil, A. and Nilsson, K. and Nilsson, O. and Reddish, M. and Suresh, M. and Koganty, R. and Fortier, S. and Baronic, L. and Berg, A. and Longenecker, M. and Hilkens, J. and Boer, M. and Karanikas, V. and McKenzie, I. and Galanina, O. and Simeon, L. and Ter-Grigoryan, A. and Belyanchikov, I. and Bovin, N. and Cao, Y. and Karsten, U. and Dai, J. and Allard, W. and Davis, G. and Yeunng, K. and Hanisch, F.G. and Lloyd, K. and Kudryashov, V. and Sikut, R. and Sikut, A. and Zhang, K. and Baeckstroem, D. and Hansson, G. and Reis, C. and Hassan, H. and Bennett, E. and Clausen, H. and Norum, L. and Varaas, T. and Kierulf, B. and Nustad, K. and Ciborowski, P. and Konitzki, W. and Magarian-Blander, J. and Finn, O.J. and Hilgers, J.
Abstract:Sixteen research groups participated in the ISOBM TD-4 Workshop in which the reactivity and specificity of 56 monoclonal antibodies against the MUC1 mucin was investigated using a diverse panel of target antigens and MUC1 mucin-related synthetic peptides and glycopeptides. The majority of antibodies (34/56) defined epitopes located within the 20-amino acid tandem repeat sequence of the MUC1 mucin protein core. Of the remaining 22 antibodies, there was evidence for the involvement of carbohydrate residues in the epitopes for 16 antibodies. There was no obvious relationship between the type of immunogen and the specificity of each antibody. Synthetic peptides and glycopeptides were analyzed for their reactivity with each antibody either by assay of direct binding (e.g. by ELISA or BiaCore) or by determining the capacity of synthetic ligands to inhibit antibody binding interactions. There was good concordance between the research groups in identifying antibodies reactive with peptide epitopes within the MUC1 protein core. Epitope mapping tests were performed using the Pepscan analysis for antibody reactivity against overlapping synthetic peptides, and results were largely consistent between research groups. The dominant feature of epitopes within the MUC1 protein core was the presence, in full or part, of the hydrophilic sequence of PDTRAPAP. Carbohydrate epitopes were less easily characterized and the most useful reagents in this respect were defined oligosaccharides, rather than purified mucin preparations enriched in particular carbohydrate moieties. It was evident that carbohydrate residues were involved in many epitopes, by regulating epitope accessibility or masking determinants, or by stabilizing preferred conformations of peptide epitopes within the MUC1 protein core. Overall, the studies, highlight concordance between groups rather than exposing inconsistencies which gives added confidence to the results of analyses of the specificity of antimucin monoclonal antibodies.
Keywords:MUC1 Mucin, Monoclonal Antibodies, Reactivity, Specificity, Affinity, Synthetic Peptides, Glycopeptides, Epitope Mapping, Animals, Mice
Source:Tumor Biology
ISSN:1010-4283
Publisher:Karger (Switzerland)
Volume:19, Suppl.1
Page Range:1-20
Date:1998
Official Publication:https://doi.org/10.1159/000056500
PubMed:View item in PubMed

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