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Expression and activity of a recombinant chimeric protein composed of pokeweed antiviral protein and of human interleukin‐2
Author(s) -
Dore Jean-Michel,
Gras Evelyne,
Wijdenes John
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(96)01493-7
Subject(s) - immunotoxin , recombinant dna , fusion protein , complementary dna , microbiology and biotechnology , biology , cytotoxic t cell , virology , chemistry , gene , biochemistry , cytotoxicity , in vitro
The pokeweed antiviral protein (PAP) has already been used to chemically construct immunotoxins. Here we tested the recombinant approach for the production of PAP‐containing cytotoxic fusion‐proteins. A cDNA encoding a mutated PAP (PAP9), which is expressed at high levels in bacteria, was fused to human interleukin‐2 (IL‐2) cDNA. The resulting PAP9–IL‐2 protein was as active as the free PAP9 in inhibiting an eukaryotic cell‐free translation system. Only the chimeric protein desaminated the 28S rRNA and inhibited translation of the CTLL‐2 cell line which expresses the IL‐2 receptor. These results show that PAP is a suitable toxin for the production of recombinant immunotoxins.