Abstract
A multitude of cell-type-specific toxins have been made by linking toxins to cell-surface binding moieties. This section focuses on the various toxins and toxin-related and toxin-derived proteins that have been used.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Pappenheimer, A.M., Jr. (1977) Diphtheria toxin. Ann. Rev. Biochem., 46, 69–94.
Moolten, F.L., and Cooperband, S.R. (1970) Selective destruction of target cells by diphtheria toxin conjugated to antibody directed against antigens on the cells. Science, 169, 68–70.
Chang, T., and Neville, D.M., Jr. (1977) Artificial hybrid protein containing a toxic protein fragment and a cell membrane receptor-binding moiety in a disulfide conjugate. II. Biochemical and biologic properties of diphtheria toxin fragment A-S-S-human placental lactogen. J. Biol. Chem., 252, 1515–1522.
Williams, D.P. et al. (1987) submitted.
Hwang, J., FitzGerald, D.J., Adhya, S., and Pastan, I. (1987) Functional domains of Pseudomonas exotoxin identified by deletion analysis of the gene expressed in E. cols. Cell, 48, 129–136.
Gilliland, D.G., Steplewski, Z., Collier, R.J., Mitchell, K.F., Tong, H.C., and Koproski, H. (1980) Antibody-directed cytotoxic agents: Use of monoclonal antibody to direct the action of toxin A chains to colorectal carcinoma cells. Proc. Natl. Acad. Sci. USA, 77, 4539–4543.
Cawley, D.B., Hershman, H.R., Gilliland, D.G., and Collier, R.J. (1980) Epidermal growth factor-toxin A chain conjugates: EGF-ricin A is a potent toxin while EGF-diphtheria fragment A is nontoxic. Cell, 22, 563–570.
Bacha, P., Murphy, J.R., and Reichlin, S. (1983) Thyrotropin-releasing hormone-diphtheria toxin-related polypeptide conjugates. Potential role of the hydrophobic domain in toxin entry. J. Biol. Chem., 258, 1565–1570.
Colombatti, M., Greenfield, L., and Youle, R.J. (1986) Cloned fragment of diphtheria toxin linked to T cell-specific antibody identifies regions of B chain active in cell entry. J. Biol. Chem., 261, 3030–3035.
Gregg, E.O., Bridges, S.H., Youle, R.J., Longo, D.L., Houston, L.L., Glennie, M.J., Stevenson, F.K., and Green, I. (1987) J. Immunol., 138, 4502–4508.
Youle, R.J., Uckun, F., Vallera, D.A., and Colombatti, M. (1986) Immunotoxins show rapid entry of diphtheria toxin but not ricin via the T3 antigen. J. Immunol., 136, 93–98.
Pappenheimer, A.M., Jr., Harper, A.A., Moynihan, M., and Brockes, J.P. (1982) Diphtheria toxin and related proteins: Effect of route of injection on toxicity and the determination of cytotoxicity for various cultured cells. J. Infect. Dis., 145, 94–102.
Godal, A., Fodstad, O., Morgan A.C., and Pihl, A. (1986) Human melanoma cell lines showing striking inherent differences in sensitivity to immunotoxins containing holotoxins. J. Natl. Cancer Inst., 77, 1247–1253.
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1988 Kluwer Academic Publishers
About this chapter
Cite this chapter
Youle, R.J. (1988). Toxin selection and modification — Overview. In: Frankel, A.E. (eds) Immunotoxins. Cancer Treatment and Research, vol 37. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1083-9_6
Download citation
DOI: https://doi.org/10.1007/978-1-4613-1083-9_6
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4612-8419-2
Online ISBN: 978-1-4613-1083-9
eBook Packages: Springer Book Archive