Molecular cloning and characterization of peroxiredoxin from Toxoplasma gondii
The Korean Journal of Parasitology
; : 133-141, 2001.
Article
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| WPRIM
| ID: wpr-94819
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WPRO
ABSTRACT
A cDNA of 1.1 kb comprising the gene encoding the peroxiredoxin of Toxoplasma gondii (TgPrx) has been cloned. The open reading frame of 591 bp was translated into a protein of 196 amino acids with a molecular mass of 25 kDa. Conserved 2 cysteine domains of Phe-Val-Cys-Pro and Glu-Val-Cys-Pro indicated TgPrx belonged to 2-Cys Prx families. TgPrx showed the highest homology with that of Arabidopsis thaliana by 53.9% followed by Entamoeba histolytica with 39.5% by the amino acid sequence alignment. Polyclonal antibody against recombinant TgPrx detected 25 kDa band in T. gondii without binding to host cell proteins. TgPrx was located in the cytoplasm of T. gondii extracellularly or intracellularly by immunofluorescence assay. The expression of TgPrx was increased as early as 30 min after the treatment with artemisinin in the intracellular stage, while no changes in those of host Prx I and TgSOD. This result implies that TgPrx may function as an antioxidant protecting the cell from the attack of reactive oxygen intermediates. It is also suggested that TgPrx is a possible target of chemotherapy.
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Asunto principal:
Peroxidasas
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Sesquiterpenos
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Toxoplasma
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Datos de Secuencia Molecular
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Secuencia de Bases
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Secuencia de Aminoácidos
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Clonación Molecular
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Técnicas de Amplificación de Ácido Nucleico
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Cisteína
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Artemisininas
Límite:
Animals
Idioma:
En
Revista:
The Korean Journal of Parasitology
Año:
2001
Tipo del documento:
Article