Korean J Parasitol.  2004 Jun;42(2):61-66. 10.3347/kjp.2004.42.2.61.

Aspartic proteases of Plasmodium vivax are highly conserved in wild isolates

• Na BK
• Lee EG
• Lee HW
• Cho SH
• Bae YA
• Kong Y
• Lee JK
• Kim TS

• KMID: 1051420
• DOI: http://doi.org/10.3347/kjp.2004.42.2.61

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.

Keyword

Plasmodium vivax; aspartic proteases; antimalarial drug

MeSH Terms

Amino Acid Sequence
Animals
Aspartic Endopeptidases/*genetics
Base Sequence
Cloning, Molecular
Conserved Sequence
DNA, Protozoan/chemistry/genetics
Human
Molecular Sequence Data
Plasmodium vivax/*enzymology/genetics/isolation & purification
Polymerase Chain Reaction
Sequence Alignment
Sequence Analysis, DNA
Support, Non-U.S. Gov't