Molecular characterization of a 2-Cys peroxiredoxin from the human malaria parasite Plasmodium falciparum

Shin ichiro Kawazu, Kanako Komaki, Naotoshi Tsuji, Satoru Kawai, Nozomu Ikenoue, Toshimitsu Hatabu, Hiroyuki Ishikawa, Yoshitsugu Matsumoto, Kunisuke Himeno, Shigeyuki Kano

Research output: Contribution to journalArticlepeer-review

48 Citations (Scopus)


We have identified the 2-Cys peroxiredoxin (PfPrx-1) from the human malaria parasite Plasmodium falciparum. The PfPrx-1 showed the highest identity at amino acid level to the type II Prx among the currently known six subfamilies of mammalian Prx. The sequence identity between the PfPrx-1 and the previously reported 1-Cys Prx of P. falciparum (PfPrx-2), which corresponded to mammalian type VI Prx, was 25%. This suggests that the parasite possesses two Prx subfamilies. The PfPrx-1 showed significant sequence similarities with those of 2-Cys peroxiredoxins of plants in the BLASTX search. This may reflect the consequences of a genetic transfer from an algal endosymbiont to the parasite nucleus during evolution. The recombinant PfPrx-1 protein (rPfPrx-1) was expressed as a histidine fusion protein in Escherichia coli and purified with Ni chromatography. The rPfPrx-1 existed as dimers under non-reducing conditions and dissociated into monomers in the presence of dithiothreitol. The PfPrx-1 protein also exists as a dimer in the parasites themselves. The reduction of the oxidized enzyme by the donation of electrons from E. coli thioredoxin (Trx)/Trx reductase system was demonstrated in its reaction with H2O2, using the rPfPrx-1 protein. These results suggested that the PfPrx-1 can act as a terminal peroxidase of the parasite Trx system. An elevated expression of the PfPrx-1 protein seen in the trophozoite, the stage with active metabolism, suggests an association of the parasite Trx system with its intracellular redox control.

Original languageEnglish
Pages (from-to)73-79
Number of pages7
JournalMolecular and Biochemical Parasitology
Issue number1
Publication statusPublished - 2001
Externally publishedYes


  • Antioxidant
  • Malaria
  • Peroxiredoxin
  • Plasmodium falciparum
  • Thioredoxin peroxidase

ASJC Scopus subject areas

  • Parasitology
  • Molecular Biology


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