Application of DsbA Signal Peptide for Soluble Expression of Leishmania infantum P4 Nuclease in E. coli

Abstract

Drugs available for treatment of Visceral Leishmaniasis (VL) are toxic and drug resistance is increasing in many parts of the world, thus it seems that vaccine development is an ideal method for prevention and control of VL. P4 nuclease of L. infantum, an amastigote stage specific protein, is considered as a good candidate for VL. Previous efforts for recombinant expression of this protein in E. coli resulted in production as inclusion body form. In the present study, the effect of DsbA signal peptide on periplasmic expression and production of soluble recombinant P4 antigen were examined. DNA extracted from L. infantum was used for amplification of P4 nuclease gene (Li-P4) by PCR. The product was cloned, sequenced and expressed in E. coli under signal sequence DsbA. The results indicated that periplasmic expression of Li-P4 gene in E coli leads to production of high levels of recombinant protein in soluble form.