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BioMed Research International
Volume 2013 (2013), Article ID 148317, 7 pages
Research Article

A Recombinant Multiepitope Protein for Hepatitis B Diagnosis

1Laboratório de Biologia Molecular, Universidade de Brasília, 70910-900 Brasília, DF, Brazil
2Laboratório de Biotecnologia de Microrganismos, Universidade Federal de São João Del-Rei, 35501-296 Divinópolis, MG, Brazil
3Laboratório de Imunopatologia, Departamento de Patologia Molecular, Universidade de Brasília, 70910-900 Brasília, DF, Brazil
4Laboratório de Biofísica, Instituto de Ciências Biológicas, Universidade de Brasília, 70910-900 Brasília, DF, Brazil
5Pós-Graduação em Ciências Genômicas e Biotecnologia, Universidade Católica de Brasília, 70910-900 Brasília, DF, Brazil

Received 7 May 2013; Revised 30 August 2013; Accepted 9 September 2013

Academic Editor: Esteban Martinez

Copyright © 2013 Marilen Queiroz de Souza et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Hepatitis B is a liver inflammation caused by hepatitis B virus (HBV) and can be diagnosed in clinical stage by hepatitis B core antibody from IgM class (anti-HBcIgM). Hepatitis B core antibody from IgG class (Anti-HBcIgG) appears quickly after IgM, reaching high titers in chronic hepatitis, and remains even after cure. Since hepatitis B core antibody (anti-HBc) is the first antibody identified and sometimes the only marker detected during the course of infection, it can be used both to indicate HBV acute infection (anti-HBc-IgM) and to identify individuals who have come into contact with the virus (anti-HBc-IgG). In this work we propose a recombinant hepatitis B core multiepitope antigen (rMEHB) to be used for diagnosis of hepatitis B. For this purpose, a synthetic gene coding for rMEHB was designed and cloned into vector pET21a with a 6xHis tag at the C-terminal. Time course induction in E. coli showed an induced protein with an apparent molecular mass of ~21 kDa. Protein purification was performed by a single step with affinity chromatography Ni-NTA. Circular dichroism spectroscopy indicated rMEHB as a thermal stable protein at pH 7.0 and 8.0. In these conditions rMEHB was successfully used to perform an enzyme linked immuno sorbent assay (ELISA) with positive and negative sera.