Parasites, Hosts and Diseases

The Korea Society for Parasitology and Tropical Medicine (대한기생충학·열대의학회)
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Aspartic proteases of Plasmodium vivax are highly conserved in wild isolates

  • Na, Byoung-Kuk (Department of Molecular Parasitology and Center for Molecular Medicine Sungkyunkwan University School of Medicine and Samsung Biomedical Research Institute) ;
  • Lee, Eung-Goo (Department of Molecular Parasitology and Center for Molecular Medicine Sungkyunkwan University School of Medicine and Samsung Biomedical Research Institute) ;
  • Lee, Hyeong-Woo (Department of Tropical and Endemic Parasitic Diseases, National Institute of Healt) ;
  • Cho, Shin-Hyeong (Department of Tropical and Endemic Parasitic Diseases, National Institute of Healt) ;
  • Bae, Young-An (Department of Molecular Parasitology and Center for Molecular Medicine Sungkyunkwan University School of Medicine and Samsung Biomedical Research Institut) ;
  • Kong, Yoon (Department of Molecular Parasitology and Center for Molecular Medicine Sungkyunkwan University School of Medicine and Samsung Biomedical Research Institut) ;
  • Lee, Jong-Koo (Bureau of Health Promotion, Ministry of Health and Welfare) ;
  • Kim, Tong-Soo (Department of Tropical and Endemic Parasitic Diseases, National Institute of Health)
  • Published : 2004.06.01
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Abstract

The plasmepsins are the aspartic proteases of malaria parasites. Treatment of aspartic protease inhibitor inhibits hemoglobin hydrolysis and blocks the parasite development in vitro suggesting that these proteases might be exploited their potentials as antimalarial drug targets. In this study, we determined the genetic variations of the aspartic proteases of Plasmodium vivax (PvPMs) of wild isolates. Two plasmepsins (PvPM4 and PvPM5) were cloned and sequenced from 20 P. vivax Korean isolates and two imported isolates. The sequences of the enzymes were highly conserved except a small number of amino acid substitutions did not modify key residues for the function or the structure of the enzymes. The high sequence conservations between the plasmepsins from the isolates support the notion that the enzymes could be reliable targets for new antimalarial chemotherapeutics.

Keywords

References

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