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Cloning of Plasmodium falciparum protein disulfide isomerase homologue by affinity purification using the antiplasmodial inhibitor 1,4‐bis{3‐[ N ‐(cyclohexyl methyl)amino]propyl}piperazine 1
Author(s) -
Florenta Isabelle,
Mouray Elisabeth,
Dali Ali Fouad,
Drobecq Hervé,
Girault Sophie,
Schrével Joseph,
Sergheraert Christian,
Grellier Philippe
Publication year - 2000
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(00)02170-0
Subject(s) - plasmodium falciparum , protein disulfide isomerase , biochemistry , isomerase , affinity chromatography , piperazine , oxidoreductase , thiol , enzyme , amino acid , biology , chemistry , microbiology and biotechnology , stereochemistry , malaria , immunology , pharmacology
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.