High Level Expression of Glycoprotein D of Herpes Simplex Virus in Escherichia Coli

Herpes simplex virus glycoprotien D gene was amplified from HSV-2 Sav strain. The D gene fragment was cloned into M13mp18 and M13mp19 and sequenced.The gD and expression vector(PWR450-1) were recombined, the recombinants could express high level corresponding beta galactosidase antigen fusion proteins in E.coli.The SDS-PAGE analysis demonstrated that the expressed fusion protein consists of 50.1% of total bacterial proteins. The immunogenicity of the product was tested with dot-ELISA and Western blot. Preliminary purification of gD galactosidase fusion protein showed that the product exhibied a purity over 90%.The results of investigation will help to study the immunogenicity of gD and produce genetic engineering vaccine of genital herpes simplex. Key words: Herpes simplex virus; Glycoprotein D