Abstract
Hepatitis B is a widespread viral disease1. In the absence of cell cultures capable of propagating the virus (HBV) an efficient vaccine has been prepared from viral envelopes isolated from the plasma of chronic carriers2–4. The major polypeptide of the envelope is one of molecular weight 25,000 which carries the surface antigen (HBsAg)5–8. Therefore, the biosynthesis of this polypeptide in Escherichia coli may offer an alternative procedure to produce HBsAg free from human proteins. Recently, the HBV genome has been cloned in E. coli9–11. Determination of its primary structure allowed the localization of the gene (called gene S) coding for HBsAg12–15 and the synthesis of the core antigen in E. coli has been reported9. We have constructed a derivative of bacteriophage lambda carrying a fusion between the β-galactosidase gene (lacZ) and the HBsAg coding sequence (λlacHBs-1). Infection of E. coli with λlacHBs-1 leads to the biosynthesis of a polypeptide of molecular weight 138,000 carrying antigenic determinants of HBV surface antigen.
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Charnay, P., Gervais, M., Louise, A. et al. Biosynthesis of hepatitis B virus surface antigen in Escherichia coli. Nature 286, 893–895 (1980). https://doi.org/10.1038/286893a0
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DOI: https://doi.org/10.1038/286893a0
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