Several fragments of the preS region of the hepatitis B virus core pro
tein were introduced into the central region of the nucleocapsid prote
in (HBcAg) of this virus. It was shown that polypeptides containing fr
agments 31-36 and 94-105 form aggregates similar to the 27-nm particle
of HBcAg and display the antigenic activity typical of both HBcAg and
the epitopes introduced. Meanwhile, introduction of fragment 133-143
(preS2 region) or a trimer of fragment 94-105 (preS1) into the central
region of HBcAg changes the hydrophobicity of the latter. A hybrid pr
otein was designed containing a fragment of preS2 at the N terminus an
d a fragment of preS1 in the central region. It was shown that the epi
tope in the central region of HBcAg is presented more efficiently than
at its N terminus if the particles retain the ability to aggregate.