Several vaccinia virus recombinants inducing the synthesis of the middle surface (M) protein of hepatitis B virus (HBV) were constructed. One of them, denoted v137, was examined in some detail. The virus replicated nearly to the same extent in various cell lines, viz. human embryo diploid fibroblast LEP and MRC-5 cells, rabbit embryo fibroblast REF cells, TK- rat RAT-2 cells, and green monkey CV-1 cells. However, the production of M protein was found considerably lower in the human LEP and MRC-5 than in the other cells examined. In addition, the kinetics of M formation were different in these two cell systems, LEP cells lagging significantly behind CV-1 cells. The low-level production of M protein in LEP cells was not increased by repeated v137 passages in LEP cells, nor by a passage in a laboratory worker accidentally infected with the v137 virus, nor by shortening the leader sequence preceding the translation initiation codon. The greater part of the M antigen was found to be cell associated, more so in the cells of human than monkey origin. From the major HBV S antigen (HBsAg) isolated from the plasma of chronically infected subjects, the antigen released by cell destruction differed by binding to polymerized human albumin. This property was utilized in ELISA to detect anti-preS2 antibody. Rabbits inoculated intradermally with the v137 virus developed antibodies reactive in this assay as well as with a synthetic peptide corresponding in the amino acids 14-34 of the NH2 terminus of the HBsAg preS2 region.

Department of Experimental Virology Institute of Sera and Vaccines Prague Czechoslovakia

Zobrazit více v PubMed

J Virol. 1987 Apr;61(4):1286-90 PubMed

Acta Virol. 1988 Sep;32(5):409-16 PubMed

Proc Natl Acad Sci U S A. 1982 Dec;79(23):7415-9 PubMed

J Virol. 1984 Mar;49(3):857-64 PubMed

Nature. 1986 Apr 10-16;320(6062):535-7 PubMed

Acta Virol. 1969 May;13(3):209-15 PubMed

Biochimie. 1988 Jan;70(1):89-97 PubMed

Exp Cell Res. 1961 Mar;23:324-34 PubMed

Virology. 1981 Aug;113(1):408-11 PubMed

Proc Natl Acad Sci U S A. 1984 Jan;81(1):193-7 PubMed

Nature. 1983 Apr 7;302(5908):490-5 PubMed

Annu Rev Immunol. 1987;5:305-24 PubMed

J Virol. 1986 Nov;60(2):337-44 PubMed

Vopr Virusol. 1988 Mar-Apr;33(2):175-9 PubMed

J Virol. 1982 Apr;42(1):100-5 PubMed

J Virol. 1987 Mar;61(3):683-92 PubMed

Proc Natl Acad Sci U S A. 1986 Dec;83(24):9338-42 PubMed

J Med Virol. 1986 Oct;20(2):111-25 PubMed

Mol Cell Biol. 1987 Jul;7(7):2538-44 PubMed

Proc Natl Acad Sci U S A. 1982 Aug;79(16):4927-31 PubMed

J Gen Virol. 1987 Aug;68 ( Pt 8):2249-52 PubMed

Virus Res. 1987 Feb;7(1):49-67 PubMed

J Natl Cancer Inst. 1973 Mar;50(3):759-66 PubMed

Hepatitis B virus proteins expressed by recombinant vaccinia viruses: influence of preS2 sequence on expression surface and nucleocapsid proteins in human diploid cells

Synthesis and immunogenicity of hepatitis B virus envelope antigen expressed by recombinant vaccinia virus. Finding of retention signal in the C-terminal portion of the preS1 domain of subtype adyw

Priming effect of recombinant vaccinia virus coding for the middle hepatitis B surface antigen