Epitope specificity of the monoclonal anticytokeratin antibody TS1

Due to their abundance in epithelial cells and deposition in necrotic regions intratumorally, cytokeratins (CKs) have been established as valuable targets for both radioimmunolocalization and radioimmunotherapy. The target epitope for the monoclonal anti-CK8 antibody, TS1, used for both experimental...

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Bibliographic Details
Published in:Cancer research (Chicago, Ill.) Ill.), 1999, Vol.59 (1), p.48-51
Main Authors: JOHANSSON, A, SANDSTRÖM, P, ULLEN, A, BEHRAVAN, G, ERLANDSSON, A, LEVI, M, SUNDSTRÖM, B, STIGBRAND, T
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Antibodies, Monoclonal - immunology
Antibody Specificity
Antineoplastic agents
Biological and medical sciences
Combined treatments (chemotherapy of immunotherapy associated with an other treatment)
Enzyme-Linked Immunosorbent Assay
Humans
Immunodominant Epitopes - genetics
Immunodominant Epitopes - immunology
Keratins - genetics
Keratins - immunology
Medical sciences
Medicin och hälsovetenskap
Molecular Sequence Data
Pharmacology. Drug treatments
Radiation therapy and radiosensitizing agent
Sequence Analysis
Treatment with physical agents
Treatment. General aspects
Tumors
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Summary:Due to their abundance in epithelial cells and deposition in necrotic regions intratumorally, cytokeratins (CKs) have been established as valuable targets for both radioimmunolocalization and radioimmunotherapy. The target epitope for the monoclonal anti-CK8 antibody, TS1, used for both experimental radioimmunolocalization and radioimmunotherapy, was determined by means of synthesis of 96 overlapping peptides that covered the entire CK8 molecule. A highly conserved peptide sequence, spanning amino acids (aa) 343-357 and covering the discontinuous epitope in the helical 2B domain, was identified. The epitope retains its helical structure, as shown with circular dichroism spectroscopy, although the length of the peptide (ie., >20 aa) is crucial for maintenance of immunoreactivity. To determine which aa residues are crucial for binding to the monoclonal antibody, alanine scanning was performed on a 26-mer covering aa 340-365, with the sequence QRGELAIKDANAKLSELEAALQRAKQ. The 26 modified peptides were evaluated using ELISA and BIAcore technology. The uniqueness of this epitope has been established by data base sequence comparisons.
ISSN:0008-5472
1538-7445
1538-7445