Molecular characterization and immunolocalization of a protein disulfide isomerase from Angiostrongylus cantonensis.
Parasitol Res
; 110(6): 2501-7, 2012 Jun.
Article
em En
| MEDLINE
| ID: mdl-22218922
ABSTRACT
Protein disulfide isomerases (PDIs), belonging to the thioredoxin superfamily, are oxidoreductases that catalyze the formation, reduction, and isomerization of disulfide bonds among cysteine residues of proteins. In this study, we report the cloning and characterization of a cDNA encoding a protein disulfide isomerase (AcPDI) from a cDNA library of fourth-stage larvae of Angiostrongylus cantonensis. The deduced amino acid sequence contains two thioredoxin domains and exhibits high identity to the homologues from other species. Quantitative real-time PCR (qRT-PCR) was performed at the third-stage larvae, fourth-stage larvae, and adult stage of A. cantonensis, and the results revealed that the AcPDI mRNA, while expressed at all three stages, is expressed at a significantly higher level in female adult worms. Results of immunohistochemical studies indicated that the AcPDI expression was specifically localized in the tegument and uterus wall of female adult worms. Biochemical analysis showed that recombinant AcPDI was biologically active in vitro and exhibited the typical biochemical functions of PDIs oxidase/isomerase and reductase activities. Collectively, these results implied that AcPDI may be a female-enriched protein and associated with the reproductive development of A. cantonensis. In addition, considering its biochemical properties, AcPDI may be involved in the formation of the cuticle of A. cantonensis.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Angiostrongylus cantonensis
/
Isomerases de Dissulfetos de Proteínas
Limite:
Animals
Idioma:
En
Ano de publicação:
2012
Tipo de documento:
Article