Oligopeptidase B from L. amazonensis: molecular cloning, gene expression analysis and molecular model.

Abstract:

: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.

journal_name

Parasitol Res

journal_title

Parasitology research

authors

de Matos Guedes HL,Carneiro MP,Gomes DC,Rossi-Bergmanmn B,Giovanni de Simone S

doi

10.1007/s00436-007-0552-5

subject

Has Abstract

pub_date

2007-09-01 00:00:00

pages

853-63

issue

4

eissn

0932-0113

issn

1432-1955

journal_volume

101

pub_type

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