Abstract

IpaD is one of the most important virulence factors in Shigella dysentriae. Recent studies showed that N-terminal region of IpaD has a major role in bacterial invasion and it could be considered as a suitable candidate for vaccine development against S. dysentriae. In this study, the gene was cloned into Ecoli in order to have sufficient amount of protein and subsequently the recombinant protein was purified. So as to optimize protein expression, Taguchi statistical method was used. After optimization of the method, Protein expression was increased by 2.2 fold compared to control. This study showed that the K2HPO4/KH2PO4 ratio and OD600nm of Induction are the main factors in the expression of the recombinant IpaD by E.coli BI21 DE3, while other variables have slight effects on the expression procedure.