Biopolym. Cell. 1985; 1(2):99-105.
Gene-Engineering Biotechnology
Expression of two variants of human hepatitis b-virus core antigen gene in Escherichia coli
1Borisova G. P., 1Kalis Ya. V., 1Dishler A. V., 1Pumpen I. P., 1Gren E. Ya., 2Tsibinogin V. V., 2Kukain P. A.
  1. Institute of Organic Synthesis, Academy of Sciences of the Latvian SSR
    Riga, USSR
  2. Institute of Microbiology, Academy of Sciences of the Latvian SSR
    Riga, USSR

Abstract

The plasmids for direct expression of human hepatitis B core antigen (HBcAg) gene in E. coli cells controlled by trp promoter are constructed. They differ in the 5'-terminal part of HBcAg gene. First or second initiated ATG-codons located in the open reading frame C are close to the Shine-Dalgarno sequence of trpL gene. An effective synthesis of poly-peptides with molecular weights 24 and 21 kD evoked by the expression of long and short variants of HBcAg gene, respectively, are shown in vitro, using the E. coli coupled transcription-translation cell-free system. The synthesis of immunologically active HBcAg occurs in bacterial cells in vivo. The approximate yields of both HBcAg variants are estimated by the competitive radioimmunoprecipitation assay.

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