The core antigen of hepatitis B virus (HBcAg) made in Escherichia coli yiel
ds particles that closely resemble the viral nucleocapsid. Extensive modifi
cations can be made to the primary structure of HBcAg without impairing par
ticle assembly. This enables other peptide sequences, including very long s
equences, to be added, substituted, or inserted into the nucleocapsid subun
it while retaining the ability to form highly immunogenic particles. These
also retain the T cell epitopes of HBcAg and constitute powerful delivery s
ystems for a diverse range of immunogenic epitopes and have significant pot
ential for development of multi-component vaccines.