Summary report on the ISOBM TD-4 Workshop: Analysis of 56 monoclonal antibodies against the MUC1 mucin. San Diego, Calif., November 17-23, 1996

M. R. Price, P. D. Rye, E. Petrakou, A. Murray, K. Brady, S. Imai, S. Haga, Y. Kiyozuka, D. Schol, M. F.A. Meulenbroek, F. G.M. Snijdewint, S. Von Mensdorff-Pouilly, R. A. Verstraeten, P. Kenemans, A. Blockzjil, K. Nilsson, O. Nilsson, M. Reddish, M. R. Suresh, R. R. KogantyS. Fortier, L. Baronic, A. Berg, M. B. Longenecker, J. Hilkens, M. Boer, V. Karanikas, I. F.C. McKenzie, O. E. Galanina, L. A. Simeoni, A. G. Ter-Grigoryan, I. M. Belyanchikov, N. V. Bovin, Y. Cao, U. Karsten, J. Dai, W. J. Allard, G. Davis, K. K. Yeung, F. G. Hanisch, K. O. Lloyd, V. Kudryashov, R. Sikut, A. Sikut, K. Zhang, D. Baeckström, G. C. Hansson, C. A. Reis, H. Hassan, E. P. Bennett, H. Claussen, L. Norum, T. Varaas, B. Kierulf, K. Nustad, P. Ciborowski, W. M. Konitzki, J. Magarian- Blander, O. J. Finn, J. Hilgers

Research output: Contribution to journalArticle

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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 PDTRPAP. 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.

Original languageEnglish (US)
Pages (from-to)1-20
Number of pages20
JournalTumor Biology
Volume19
Issue numberSUPPL. 1
StatePublished - Dec 1998

Fingerprint

Mucins
Epitopes
Monoclonal Antibodies
Education
Antibodies
Peptides
Carbohydrates
Glycopeptides
Amino Acid Repetitive Sequences
Proteins
Research
Epitope Mapping
Tandem Repeat Sequences
Antibody Specificity
Oligosaccharides
Enzyme-Linked Immunosorbent Assay
Ligands
Antigens

Keywords

  • Epitope mapping
  • MUC1 mucin
  • Monoclonal antibodies
  • Reactivity, specificity and affinity
  • Synthetic peptides and glycopeptides

ASJC Scopus subject areas

  • Cancer Research

Cite this

Price, M. R., Rye, P. D., Petrakou, E., Murray, A., Brady, K., Imai, S., ... Hilgers, J. (1998). Summary report on the ISOBM TD-4 Workshop: Analysis of 56 monoclonal antibodies against the MUC1 mucin. San Diego, Calif., November 17-23, 1996. Tumor Biology, 19(SUPPL. 1), 1-20.

Summary report on the ISOBM TD-4 Workshop : Analysis of 56 monoclonal antibodies against the MUC1 mucin. San Diego, Calif., November 17-23, 1996. / Price, M. R.; Rye, P. D.; Petrakou, E.; Murray, A.; Brady, K.; Imai, S.; Haga, S.; Kiyozuka, Y.; Schol, D.; Meulenbroek, M. F.A.; Snijdewint, F. G.M.; Von Mensdorff-Pouilly, S.; Verstraeten, R. A.; Kenemans, P.; Blockzjil, A.; Nilsson, K.; Nilsson, O.; Reddish, M.; Suresh, M. R.; Koganty, R. R.; Fortier, S.; Baronic, L.; Berg, A.; Longenecker, M. B.; Hilkens, J.; Boer, M.; Karanikas, V.; McKenzie, I. F.C.; Galanina, O. E.; Simeoni, L. A.; Ter-Grigoryan, A. G.; Belyanchikov, I. M.; Bovin, N. V.; Cao, Y.; Karsten, U.; Dai, J.; Allard, W. J.; Davis, G.; Yeung, K. K.; Hanisch, F. G.; Lloyd, K. O.; Kudryashov, V.; Sikut, R.; Sikut, A.; Zhang, K.; Baeckström, D.; Hansson, G. C.; Reis, C. A.; Hassan, H.; Bennett, E. P.; Claussen, H.; Norum, L.; Varaas, T.; Kierulf, B.; Nustad, K.; Ciborowski, P.; Konitzki, W. M.; Magarian- Blander, J.; Finn, O. J.; Hilgers, J.

In: Tumor Biology, Vol. 19, No. SUPPL. 1, 12.1998, p. 1-20.

Research output: Contribution to journalArticle

Price, MR, Rye, PD, Petrakou, E, Murray, A, Brady, K, Imai, S, Haga, S, Kiyozuka, Y, Schol, D, Meulenbroek, MFA, Snijdewint, FGM, Von Mensdorff-Pouilly, S, Verstraeten, RA, Kenemans, P, Blockzjil, A, Nilsson, K, Nilsson, O, Reddish, M, Suresh, MR, Koganty, RR, Fortier, S, Baronic, L, Berg, A, Longenecker, MB, Hilkens, J, Boer, M, Karanikas, V, McKenzie, IFC, Galanina, OE, Simeoni, LA, Ter-Grigoryan, AG, Belyanchikov, IM, Bovin, NV, Cao, Y, Karsten, U, Dai, J, Allard, WJ, Davis, G, Yeung, KK, Hanisch, FG, Lloyd, KO, Kudryashov, V, Sikut, R, Sikut, A, Zhang, K, Baeckström, D, Hansson, GC, Reis, CA, Hassan, H, Bennett, EP, Claussen, H, Norum, L, Varaas, T, Kierulf, B, Nustad, K, Ciborowski, P, Konitzki, WM, Magarian- Blander, J, Finn, OJ & Hilgers, J 1998, 'Summary report on the ISOBM TD-4 Workshop: Analysis of 56 monoclonal antibodies against the MUC1 mucin. San Diego, Calif., November 17-23, 1996', Tumor Biology, vol. 19, no. SUPPL. 1, pp. 1-20.
Price, M. R. ; Rye, P. D. ; Petrakou, E. ; Murray, A. ; Brady, K. ; Imai, S. ; Haga, S. ; Kiyozuka, Y. ; Schol, D. ; Meulenbroek, M. F.A. ; Snijdewint, F. G.M. ; Von Mensdorff-Pouilly, S. ; Verstraeten, R. A. ; Kenemans, P. ; Blockzjil, A. ; Nilsson, K. ; Nilsson, O. ; Reddish, M. ; Suresh, M. R. ; Koganty, R. R. ; Fortier, S. ; Baronic, L. ; Berg, A. ; Longenecker, M. B. ; Hilkens, J. ; Boer, M. ; Karanikas, V. ; McKenzie, I. F.C. ; Galanina, O. E. ; Simeoni, L. A. ; Ter-Grigoryan, A. G. ; Belyanchikov, I. M. ; Bovin, N. V. ; Cao, Y. ; Karsten, U. ; Dai, J. ; Allard, W. J. ; Davis, G. ; Yeung, K. K. ; Hanisch, F. G. ; Lloyd, K. O. ; Kudryashov, V. ; Sikut, R. ; Sikut, A. ; Zhang, K. ; Baeckström, D. ; Hansson, G. C. ; Reis, C. A. ; Hassan, H. ; Bennett, E. P. ; Claussen, H. ; Norum, L. ; Varaas, T. ; Kierulf, B. ; Nustad, K. ; Ciborowski, P. ; Konitzki, W. M. ; Magarian- Blander, J. ; Finn, O. J. ; Hilgers, J. / Summary report on the ISOBM TD-4 Workshop : Analysis of 56 monoclonal antibodies against the MUC1 mucin. San Diego, Calif., November 17-23, 1996. In: Tumor Biology. 1998 ; Vol. 19, No. SUPPL. 1. pp. 1-20.
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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 PDTRPAP. 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.",
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T1 - Summary report on the ISOBM TD-4 Workshop

T2 - Analysis of 56 monoclonal antibodies against the MUC1 mucin. San Diego, Calif., November 17-23, 1996

AU - Price, M. R.

AU - Rye, P. D.

AU - Petrakou, E.

AU - Murray, A.

AU - Brady, K.

AU - Imai, S.

AU - Haga, S.

AU - Kiyozuka, Y.

AU - Schol, D.

AU - Meulenbroek, M. F.A.

AU - Snijdewint, F. G.M.

AU - Von Mensdorff-Pouilly, S.

AU - Verstraeten, R. A.

AU - Kenemans, P.

AU - Blockzjil, A.

AU - Nilsson, K.

AU - Nilsson, O.

AU - Reddish, M.

AU - Suresh, M. R.

AU - Koganty, R. R.

AU - Fortier, S.

AU - Baronic, L.

AU - Berg, A.

AU - Longenecker, M. B.

AU - Hilkens, J.

AU - Boer, M.

AU - Karanikas, V.

AU - McKenzie, I. F.C.

AU - Galanina, O. E.

AU - Simeoni, L. A.

AU - Ter-Grigoryan, A. G.

AU - Belyanchikov, I. M.

AU - Bovin, N. V.

AU - Cao, Y.

AU - Karsten, U.

AU - Dai, J.

AU - Allard, W. J.

AU - Davis, G.

AU - Yeung, K. K.

AU - Hanisch, F. G.

AU - Lloyd, K. O.

AU - Kudryashov, V.

AU - Sikut, R.

AU - Sikut, A.

AU - Zhang, K.

AU - Baeckström, D.

AU - Hansson, G. C.

AU - Reis, C. A.

AU - Hassan, H.

AU - Bennett, E. P.

AU - Claussen, H.

AU - Norum, L.

AU - Varaas, T.

AU - Kierulf, B.

AU - Nustad, K.

AU - Ciborowski, P.

AU - Konitzki, W. M.

AU - Magarian- Blander, J.

AU - Finn, O. J.

AU - Hilgers, J.

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AB - 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 PDTRPAP. 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.

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KW - Monoclonal antibodies

KW - Reactivity, specificity and affinity

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