Aspartic proteases of Plasmodium vivax are highly conserved in wild isolates
The Korean Journal of Parasitology
;
: 61-66, 2004.
Artigo
em Inglês
| 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.
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Plasmodium vivax
/
Dados de Sequência Molecular
/
Sequência de Bases
/
Reação em Cadeia da Polimerase
/
Ácido Aspártico Endopeptidases
/
DNA de Protozoário
/
Alinhamento de Sequência
/
Sequência de Aminoácidos
/
Clonagem Molecular
/
Análise de Sequência de DNA
Limite:
Animais
/
Humanos
Idioma:
Inglês
Revista:
The Korean Journal of Parasitology
Ano de publicação:
2004
Tipo de documento:
Artigo
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