Expression of Antibacterial Peptide CM4 in Escherichia coli Fused with Human Soluble B Lymphocyte Stimulator Activing Factor

To explore the expression and function of antibacterial peptide CM4, the expression and biological activity of recombinant fusion protein CM4–hsBAFF were studied. The human soluble B lymphocyte stimulator activing factor (hsBAFF) gene was fused to the sequence encoding CM4 to construct an expression vector pET28a (+)/CM4–hsBAFF. The recombinant protein was high expression of soluble recombinant protein in Escherichia coli cells, and existed in the supernatant after sonication. Recombinant fusion protein which was purified through size-exclusion chromatography was identified by SDS-PAGE and Western blot analysis. SDS-PAGE and Western blot indicated that recombinant protein was secreted as a protein of around 22.0kDa2 and can be specially recognized anti-hsBAFF antibody. The recombinant protein can be expressed and displays antimicrobial activity.