Expression and activity of a recombinant chimeric protein composed of pokeweed antiviral protein and of human interleukin‐2

FEBS Letters

Wijdenes, John¹  Gras, Evelyne¹  Dore, Jean-Michel¹ 

[1] Diaclone, 1 Boulevard A. Fleming, BP 1937, 25020 Besançon Cedex, France

关键词: Pokeweed antiviral protein;    Recombinant cytotoxic fusion protein;    Inhibition of translation;    N-glycosidase activity;   

DOI  :  10.1016/S0014-5793(96)01493-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown