Heterologous expression and functional characterization of thioredoxin from Fasciola hepatica

The full thioredoxin coding sequence from Fasciola hepatica has been cloned into the pGEX-2T expression vector and produced in Escherichia coli as a f usion protein. The recombinant protein proved to be biologically active, us ing an insulin reduction assay, and was also able to activate thioredoxin p eroxidase from F. hepatica. These observations suggest that this protein co uld participate in a redox cascade involved in the maintenance of cell home ostasis as well as in parasite protection against reactive oxygen species p roduced by the host.