Expression of α-β1-β2-ε Soluble Fusion Protein of Clostridium perfringens in Escherichia coli and its Immunogenicity in Mice

Currently, there is an urgent need to develop genetically engineered multivalent subunit vaccines or DNA vaccines to provide protection against infection of multiple types of Clostridium perfringens bacteria. Toward this end, in this study, a set of molecular biotechnologies were used to efficient express and obtain soluble fusion protein of alpha-beta1-beta2-epsilon-toxin (α-β1-β2-ε-toxin) derived from C. perfringens in Escherichia coli. A soluble fusion protein of α-β1-β2-ε-toxin was obtained for the first time with efficient expression in Escherichia coli system by conducting codon optimization, removing the signal peptide, selecting sequences of higher hydrophilicity and antigenicity, removing the lethal gene and optimizing the expression conditions. Noticeable rise of antibody level was detected in the serum of mice after immunization with the expressed protein. The survival rate of the immunized mice during the 7-day challenge period was 100% in the cases of C. perfringens types A, B, C and D.