Oligopeptidase B from L. amazonensis: molecular cloning, gene expression analysis and molecular model.
Parasitol Res
; 101(4): 853-63, 2007 Sep.
Article
en En
| MEDLINE
| ID: mdl-17530480
Serine oligopeptidases of trypanosomatids are emerging as important virulence factors and therapeutic targets in trypanosome infections. A complete open reading frame of oligopeptidase B from Leishmania amazonensis was amplified with polymerase chain reaction with gradient annealing temperatures using primers designed for the oligopeptidase B gene from L. major. The 2,196-bp fragment coded for a protein of 731 amino acids with a predicted molecular mass of 83.49 KDa. The encoded protein (La_OpB) shares a 90% identity with oligopeptidases of L. major and L. infantum, 84% with L. braziliensis, and approximately 62 identity with Trypanosoma peptidases. The oligopeptidase B gene is expressed in all cycle stages of L. amazonensis. The three dimensional model of La_OpB was obtained by homology modeling based on the structure of prolyl oligopeptidases. We mapped a La_OpB model that presents a greater negative charge than prolyl oligopeptidases; our results suggest a difference in the S2 subsite when compared to oligopeptidases B from Trypanosoma and bacterial oligopeptidases B. The La_OpB model serves as a starting point for its exploration as a potential target source for a rational chemotherapy.
Buscar en Google
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Serina Endopeptidasas
/
Modelos Moleculares
/
Regulación de la Expresión Génica
/
Clonación Molecular
/
Leishmania
Tipo de estudio:
Prognostic_studies
Límite:
Animals
Idioma:
En
Revista:
Parasitol Res
Asunto de la revista:
PARASITOLOGIA
Año:
2007
Tipo del documento:
Article
País de afiliación:
Brasil
Pais de publicación:
Alemania