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Aspartic proteases of Plasmodium vivax are highly conserved in wild isolates

이종구|김동수|이형우|이응구|조신형|배영안|공윤|나병석
대한기생충학ㆍ열대의학회 (The Korean Society For Parasitology and Tropical Medicine)|2004.06|Parasites, Hosts and Diseases|제42권 제2호|pp. 61-66

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참고문헌

주제분류예방의학/직업환경의학

초록

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 an 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.

참고문헌 (19)

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