Increased Refolding Yield of Disulfide Bond Bridged Fab-Toxin Homodimers by the Insertion of CH3 Domains

• Published in: Journal of microbiology and biotechnology Vol. 16; no. 7; pp. 1104 - 1110
• Main Authors: Song, J.W. (Korea University, Seoul, Republic of Korea), Won, J.S. (Korea University, Seoul, Republic of Korea), Lee, Y.C. (Korea University, Seoul, Republic of Korea), Choe, M.H. (Korea University, Seoul, Republic of Korea), E-mail: choemh@korea.ac.kr
• Format: Journal Article
• Language: English
• Published: Seoul Korean Society for Applied Microbiology 01.07.2006; 한국미생물·생명공학회
• Subjects: antibody refolding; B3 antibody; Biological and medical sciences; Biotechnology; constant domain of heavy chain; dimer; divalent antibody-toxin; Fundamental and applied biological sciences. Psychology; Pseudomonas exotoxin A; Recombinant antibody-toxin; TOXICIDAD; TOXICITE; TOXICITY; 생물학; Pseudomonadales; Heavy peptide chain; Antibody; Refolding; antibody refolding; dimer; Cytotoxicity; Fab-Fragment; Pseudomonas; Pseudomonas exotoxin A; Toxin; Recombinant antibody-toxin; constant domain of heavy chain; Disulfide bond; Bacteria; Pseudomonadaceae; divalent antibody-toxin; Yield; Exotoxin; Recombinant protein; B3 antibody
• ISSN: 1017-7825

Recombinant antibody-toxin is a bifunctional protein that binds and kills a target cell expressing a specific antigen on the surface of the cell, and its structure is chimeric, in which a toxin is fused to an antigen-binding domain such as scFv or Fab. Divalent antibody-toxin molecules showed higher cytotoxicities against cancer cell lines than monovalent molecules. However, the yields of the divalent molecules were very low. In this study, we introduced the CH2, CH3, or CH2-CH3 (=Fc) domain of antibody in the middle of the Fab-toxin between the hinge region of human IgG1 and the toxin domain to increase the yield.