Aspartic proteases of Plasmodium vivax are highly conserved in wild isolates.
10.3347/kjp.2004.42.2.61
- Author:
Byoung Kuk NA
;
Eung Goo LEE
;
Hyeong Woo LEE
;
Shin Hyeong CHO
;
Young An BAE
;
Yoon KONG
;
Jong Koo LEE
;
Tong Soo KIM
- Publication Type:Original Article ; Research Support, Non-U.S. Gov't
- Keywords:
Plasmodium vivax;
aspartic proteases;
antimalarial drug
- MeSH:
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
- From:The Korean Journal of Parasitology
2004;42(2):61-66
- CountryRepublic of Korea
- Language:English
-
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.
