Aspartic proteases of Plasmodium vivax are highly conserved in wild isolates
The Korean Journal of Parasitology
;
: 61-66, 2004.
Article
in English
| WPRIM
| ID: wpr-188036
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Plasmodium vivax
/
Molecular Sequence Data
/
Base Sequence
/
Polymerase Chain Reaction
/
Aspartic Acid Endopeptidases
/
DNA, Protozoan
/
Sequence Alignment
/
Amino Acid Sequence
/
Cloning, Molecular
/
Sequence Analysis, DNA
Limits:
Animals
/
Humans
Language:
English
Journal:
The Korean Journal of Parasitology
Year:
2004
Type:
Article
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