Design and prokaryotic expression of a multi-epitope assembly peptides (MAP) derived from herpes simplex virus type Ⅱ glycoprotein

摘要

To design a Multi-Epitope Assembly Peptides (MAP) derived from herpes simplex virus type II glycoprotein( HSV2), cloning and fusion expression of the peptides in Escherichia coli by genetic engineering technology. B cell Antigenic epitope analysis, on glycoproteins from HSV2, was based on related software. CD4+T cell Antigenic epitope analysis, on glycoproteins from HSV2, based on other related software. The whole eleven epitopes were connected by linker. Spatial structure of the random Assembly Peptides was predicted by the software. The selected sequence was chemically synthesized and cloned into and inserted into the E. coli expression vector pET27b( + ). The epitope independence of assembly was designed successfully, SDS-PAGE showed that a band corresponding to a protein of 33 kDa was obtained. The way of obtaining spatial structure of MAP by the sofeware was feasible, The sequence of recombinant protein may be applied for further study for the function of candidates vaccine of HSV2.