Production and secretion in Escherichia coli of hepatitis b virus pre-S2 antigen as fusion proteins with β-lactamase

H. Kadokura, K. Yoda, M. Imai, M. Yamasaki

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

The diagnostically important surface antigen pre-S2 of hepatitis B virus was produced in large amounts in the periplasmic space of Escherichia coli. The DNA fragments (pre-S2) coding the pre-S2 antigen were tandemly duplicated or triplicated and ligated in the same reading frame to a fragment containing the promoter and the signal sequence of the alkaline phosphatase-coding gene (phoA) of E. coli. Further, a DNA fragment (bla) coding mature β-lactamase was joined to the region coding the C terminus of the pre-S2 repeat to stabilize the gene product. Upon induction of the phoA-(pre-S2)3-bla fusion gene, the fusion protein was produced at up to 30% of the total cellular protein. Fractionation of the cellular components and trypsin accessibility of the product showed that the antigen was secreted in the periplasm and formed inclusion bodies there. The signal sequence of alkaline phosphatase was found to be correctly processed in E. coli.

Original languageEnglish
Pages (from-to)2742-2747
Number of pages6
JournalApplied and environmental microbiology
Volume56
Issue number9
DOIs
Publication statusPublished - 1990
Externally publishedYes

ASJC Scopus subject areas

  • Biotechnology
  • Food Science
  • Applied Microbiology and Biotechnology
  • Ecology

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