• Korean Journal of Microbiology
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• v.28 no.1
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• pp.6-12
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• 1990

The preS2 wequence of an adr hepatitis B virus was cloned and expressed in Escherichia coli as a $\beta$-galactosidase fusion polypeptide. Recombinant preS2 product interacted with the preS2-specific monoclonal antibody H8 which was induced by surface antigen particles isolated from a Korean gepatitis patient. The H8 showed only a minor cross-reactivity with recombinant preS2 product of adw2 subtype. Determination of nucleotide sequence of the adr preS2 revealed that twelve amino acid residue substitutions between adr and adw2 subtype sequences. The antigenic determinant to H8 must include some of these differences.

• Korean Journal of Microbiology
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• v.28 no.1
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• pp.13-18
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• 1990

A DNA sequence encoding the adr subtype preS2 region of hepatitis B virus envelope protein was fused to 5' end of lacZ gene yielding a plasmid pTSZ, in order to produce a preS2-$\beta$-galactosidase fusion protein. Serial deletions from 3' and 5' end of preS2 were constructed in plasmids, which were expressed and their antigenicities were examined with the monoclonal antibody H8. Deletions from amino and carboxy terminal to certain points did not affect the antigenicity, but the longer deletions destroyed the antigenicity. End points of deleted preS2 sequence were determined by DNA sequencing. As a result, each end of preS2 epitope was located in the region of amino acid residue 130-132 and 140-142, respectively. Residue 143 may be supplementary for antigenic epitope since the deletion from carboxy terminal to residue 143 revealed partial defect of antigenicity. In the interval of antigenic epitope the amino acid differences between adr and adw2 subtype occurred ar residue 130, 132, and 141. This result indicated that one or more of the three residues are responsible for the binding specificity of monoclonal antibody H8 to adr subtype preS2 fusion protein.