Production and characterization of an anti-(MUC1 mucin) recombinant diabody |
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| Authors: | Graeme Denton Kevin Brady Benny K C Lo Andrea Murray C Rosamund L Graves Owen D M Hughes Saul J B Tendler Charles A Laughton Michael R Price |
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| Institution: | (1) Cancer Research Laboratories, School of Pharmaceutical Sciences, University of Nottingham, University Park, Nottingham NG7 2RD, UK, GB;(2) Laboratory of Biophysics and Surface Analysis, School of Pharmaceutical Sciences, University of Nottingham, Nottingham, UK, GB;(3) Department of Surgery, City Hospital, Nottingham, UK, GB;(4) Department of Urology, City Hospital, Nottingham, UK, GB |
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| Abstract: | 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 (Gly4Ser)3, using polymerase-chain-reaction-based strategies, forces variable heavy (VH) and light (VL) 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.
Received: 16 September 1998 / Accepted: 2 December 1998 |
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| Keywords: | MUC1 Mucin Diabody scFv Immunotherapy |
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