Construction and High Expression of a Recombinant Amino-Proximal HSV-2 Glycoprotein B Polypeptide with Immunogenicity in Escherichia coli

Recombinant HSV-2 glycoprotein B amino-proximal polypeptide, a new designed polypeptide with potential immunogenic effect in vivo, was engineered. It is composed of thioredoxin and HSV-2 glycoprotein B amino-proximal segment. The recombinant gene was then highly expressed in Escherichia coli. Furthermore, the expressed fusion protein could effectively prevent degradation of polypeptide, and purified fusion protein could effectively stimulate neutralization antibody after immunizing mice. The selected antibody from antibody library constructed with high titer antiserum spleen cells of mice had very different ability to neutralize the HSV-2 in vitro. In this study, we provide an approach to produce thioredoxin and HSV-2 glycoprotein B amino terminus polypeptide fusion protein, which could using as a potential and novel target for structure based drug designing to control the infections of HSV-2.