Higher cytotoxicity of divalent antibody-toxins than monovalent antibody-toxins
- Authors
- Won, JaeSeon; Nam, PilWon; Lee, YongChan; Choe, MuHyeon
- Issue Date
- 24-Apr-2009
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- Divalent antibody-toxin; Recombinant antibody refolding; Avidity; Cytotoxicity; Pseudomonas exotoxin A
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.382, no.1, pp.15 - 20
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 382
- Number
- 1
- Start Page
- 15
- End Page
- 20
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/120204
- DOI
- 10.1016/j.bbrc.2009.02.091
- ISSN
- 0006-291X
- Abstract
- Recombinant antibody-toxins are constructed via the fusion of a "carcinorna-specific" antibody fragment to a toxin. Due to the high affinity and high selectivity of the antibody fragments, antibody-toxins can bind to surface antigens on cancer cells and kill them without harming normal cells [L.H. Pai, J.K. Batra, D.J. FitzGerald, M.C. Willingham, I. Pastan, Anti-tumor activities of immunotoxins made of monoclonal antibody 133 and various forms of Pseudonionas exotoxin, Proc. Natl. Acad. Sci. USA 88 (1991) 3358-3362]. In this study, we constructed the antibody-toxin, Fab-SWn-PE38, with SWn (n = 3, 6, 9) sequences containing n-time repeated (G4S) between the Fab fragment and PE38 (38 kDa truncated form of Pseudomonas exotoxin A). The SWn sequence also harbored one cysteine residue that Could form a disulfide bridge between two Fab-SWn-PE38 monomers. We assessed the cytotoxicity of the monovalent (Fab-SWn-PE38), and divalent ([Fab-SWn-PE38](2)) anti body-toxins. The cytotoxicity of the dimer against the CRL1739 cell line was approximately 18.8-fold higher than that of the monomer on the ng/ml scale, which was approximately 37.6-fold higher on the pM scale. These results strongly indicate that divalency provides higher cytotoxicity for an antibody-toxin. (C) 2009 Published by Elsevier Inc.
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