P. Pumpens et E. Grens, Hepatitis B core particles as a universal display model: a structure-function basis for development, FEBS LETTER, 442(1), 1999, pp. 1-6
Because it exhibits a remarkable capability to accept mutational interventi
on and undergo correct folding and self-assembly in all viable prokaryotic
and eukaryotic expression systems, hepatitis B core (HBc) protein has been
favored over other proposed particulate carriers. Structurally, the unusual
alpha-helical organization of HBc dimeric units allows introduction of for
eign peptide sequences into several areas of HBc shells, including their mo
st protruding spikes, Progress toward full resolution of the spatial struct
ure as well as accumulation of chimeric HBc-based structures has brought cl
oser the knowledge-based design of future vaccines, gene therapy tools and
other artificial particulate objects. (C) 1999 Federation of European Bioch
emical Societies.