Cloning of Plasmodium falciparum protein disulfide isomerase homologue by affinity purification using the antiplasmodial inhibitor 1,4‐bis{3‐[N‐(cyclohexyl methyl)amino]propyl}piperazine1

FEBS Letters

Mouray, Elisabeth¹  Dali Ali, Fouad¹  Drobecq, Hervé²  Sergheraert, Christian²  Girault, Sophie²  Florenta, Isabelle¹  Grellier, Philippe¹  Schrével, Joseph¹ 

[1]Laboratoire de Biologie et Evolution des Parasites, FR CNRS 63, Muséum National d'Histoire Naturelle 61, rue Buffon, 75005 Paris, France

[2]UMR 8525 CNRS, Université de Lille II, Institut de Biologie et Institut Pasteur de Lille 1, rue du Professeur Calmette, P.O. Box 447, 59021 Lille, France

关键词: Malaria;    Thiol metabolism;    Antiplasmodial inhibitor;    Protein disulfide isomerase;    Plasmodium falciparum;    CQ;    chloroquine;    ER;    endoplasmic reticulum;    PDI;    protein disulfide isomerase;    RT-PCR;    reverse transcription-polymerase chain reaction;   

DOI  :  10.1016/S0014-5793(00)02170-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A series of 10 1,4-bis(3-aminopropyl)piperazine compounds was found to display antiplasmodial activity with 50% growth inhibition between 30 and 250 nM, on three Plasmodium falciparum strains differently sensitive to chloroquine. By affinity chromatography using one of these compounds, a 52-kDa protein was isolated from P. falciparum, microsequenced and cloned. It corresponded to a single copy gene encoding a 453 amino acid protein displaying the typical features of protein disulfide isomerases, a thiol metabolizing enzyme belonging to the thiol: disulfide oxidoreductase superfamily, which was not previously described in malarial species.

【 授权许可】

Unknown