Aspartic proteases of Plasmodium vivax are highly conserved in wild isolates.
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.
Na
Byoung-Kuk
BK
Department of Molecular Parasitology and Center for Molecular Medicine, Sungkyunkwan University School of Medicine and Samsung Biomedical Research Institute, Suwon 440-746, Korea. nihkim@nih.go.kr
Lee
Eung-Goo
EG
Lee
Hyeong-Woo
HW
Cho
Shin-Hyeong
SH
Bae
Young-An
YA
Kong
Yoon
Y
Lee
Jong-Koo
JK
Kim
Tong-Soo
TS
D000595:Amino Acid Sequence; D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000235:genetics*; D001483:Base Sequence; D003001:Cloning, Molecular; D017124:Conserved Sequence; D016054:DNA, Protozoan / Q000737:chemistry / Q000235:genetics; D006801:Humans; D008969:Molecular Sequence Data; D010966:Plasmodium vivax / Q000201:enzymology* / Q000235:genetics / Q000302:isolation & purification; D016133:Polymerase Chain Reaction; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA
D016054:DNA, Protozoan; D016282:Aspartic Acid Endopeptidases