Production and characterization of an anti-(MUC1 mucin) recombinant diabody

A recombinant diabody fragment based on the anti-MUC1 monoclonal antibody, C595 has been produced in a bacterial expression system. Substitution of a 7-amino-acid linker sequence (Gly6Ser) for the original single-chain (sc)Fv 15-amino-acid linker (Gly4-Ser)3, using polymerase-chain-reaction-based st...

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Bibliographic Details
Published in:Cancer Immunology, Immunotherapy Immunotherapy, 1999-04, Vol.48 (1), p.29-38
Main Authors: DENTON, G, BRADY, K, LO, B. K. C, MURRAY, A, GRAVES, C. R. L, HUGHES, O. D. M, TENDLER, S. J. B, LAUGHTON, C. A, PRICE, M. R
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Antibodies, Bispecific - biosynthesis
Antibodies, Bispecific - chemistry
Antibodies, Bispecific - genetics
Antibodies, Monoclonal - biosynthesis
Antibodies, Monoclonal - genetics
Antibodies, Monoclonal - immunology
Antibody Specificity
Antineoplastic agents
Biological and medical sciences
Dimerization
Electrophoresis, Polyacrylamide Gel
Enzyme-Linked Immunosorbent Assay
Humans
Immunoglobulin Fragments - biosynthesis
Immunoglobulin Fragments - genetics
Immunoglobulin Fragments - immunology
Immunotherapy
Medical sciences
Mice
Models, Molecular
Molecular Sequence Data
MUC1 protein
mucin
Mucin-1 - genetics
Mucin-1 - immunology
Original
Pharmacology. Drug treatments
Polymerase Chain Reaction
Protein Conformation
Recombinant Proteins - biosynthesis
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Sequence Homology, Amino Acid
Tumor Cells, Cultured
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Description
Summary:A recombinant diabody fragment based on the anti-MUC1 monoclonal antibody, C595 has been produced in a bacterial expression system. Substitution of a 7-amino-acid linker sequence (Gly6Ser) for the original single-chain (sc)Fv 15-amino-acid linker (Gly4-Ser)3, using polymerase-chain-reaction-based strategies, forces variable heavy (V(H)) and light (V(L)) domains to pair with complementary domains on neighbouring scFv molecules, forming a scFv dimer (diabody). This recombinant protein shows similar binding characteristics to the parental C595 monoclonal antibody. The ability to bind to MUC1 mucin on carcinoma cell surfaces will allow its potential as a diagnostic and therapeutic reagent of clinical utility to be investigated.
ISSN:0340-7004
1432-0851
DOI:10.1007/s002620050545