Letters in Drug Design & Discovery

G. Perry
University of Texas
San Antonio, TX
USA
Email: lddd@benthamscience.org

Back

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

Author(s): Xu Ning, Tu Jingjing, Wang Xian Yan, Xu Fang.

Abstract:

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.

Keywords: HSV-2, glycoprotein B, High expression, prokaryotic expression, gB polypeptide segments, ulcerative blisters, Aciclovir, glycoproteins, potential immunogenic effect, thioredoxin

Order Reprints Order Eprints Rights & PermissionsPrintExport

Article Details

VOLUME: 9
ISSUE: 8
Year: 2012
Page: [809 - 814]
Pages: 6
DOI: 10.2174/157018012802652958
Price: $58