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

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Abstract

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
Volume116
Issue number1
DOIs
Publication statusPublished - Aug 14 2001
Externally publishedYes

Keywords

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

ASJC Scopus subject areas

  • Parasitology
  • Molecular Biology

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  • Cite this

    Kawazu, S. I., Komaki, K., Tsuji, N., Kawai, S., Ikenoue, N., Hatabu, T., Ishikawa, H., Matsumoto, Y., Himeno, K., & Kano, S. (2001). Molecular characterization of a 2-Cys peroxiredoxin from the human malaria parasite Plasmodium falciparum. Molecular and Biochemical Parasitology, 116(1), 73-79. https://doi.org/10.1016/S0166-6851(01)00308-5