Premium
Characterization and receptor specific toxicity of two diphtheria toxin‐related interleukin‐3 fusion proteins DAB 389 –mIL‐3 and DAB 389 –(Gly 4 Ser) 2 ‐mIL‐3
Author(s) -
Liger Dominique,
vanderSpek Johanna C,
Gaillard Carole,
Cansier Christophe,
Murphy John R,
Leboulch Philippe,
Gillet Daniel
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00243-3
Subject(s) - diphtheria toxin , fusion protein , microbiology and biotechnology , receptor , toxicity , toxin , chemistry , cytotoxic t cell , antibody , cell culture , interleukin 2 , biology , immunology , in vitro , biochemistry , recombinant dna , genetics , organic chemistry , gene
We have constructed two fusion proteins, DAB 389 –mIL‐3 and DAB 389 ‐(Gly 4 Ser) 2 –mIL‐3, in which the receptor‐binding domain of diphtheria toxin is replaced by mouse interleukin‐3 (IL‐3). Cytotoxic activity of the fusion toxins was observed on three out of six cell lines assayed. This toxicity was mediated through binding to the IL‐3 receptor as it was inhibited in a dose‐dependent manner with murine IL‐3 or anti‐IL‐3 neutralizing antibodies. DAB 389 –(Gly 4 Ser) 2 ‐mIL‐3 was up to 5 times more toxic than DAB 389 –mIL‐3, depending on the cell line (0.8×10 −10 M