K. Parker

TL;DR: A synthetic peptide analog is recognized by both cell receptors and anti-HBV antibodies and elicits antibodies reacting with native HBV, and is a promising immunogen expected to elicit protective antibodies based on the concept of the attachment blockade pathway of virus neutralization.

TL;DR: In vitro neutralization of the virus by rabbit antiserum to the peptide was assayed in chimpanzees and the animals did not develop hepatitis B, establishing the role of preS domains in the process of virus neutralization and the potential of synthetic preS analogues for hepatitis B vaccination.

TL;DR: Monoclonal antibodies specific for the pre-S region of the hepatitis B virus (HBV) envelope protein were prepared using HBV particles of hepatitis B surface antigens (HBsAg) as immunogens and reacted in Western blot analyses and in ELISA withPre-S2 sequences of the HBV envelope protein.

TL;DR: Results presented here show that antisera raised against synthetic peptide analogs carrying the immunodominant epitope of the preS1 and preS2 sequence, respectively, and corresponding to two HBV subtypes, adw2 and ayw, each recognized preS ones specific epitopes on all serological subtypes of the HBV envelope protein.

TL;DR: Results presented here highlight those subregions of the preS sequence which are the most essential for the antigenicity and immunogenicity of HBV.