Hepatitis B core particles as a universal display model: a structure-function basis for development

Citation
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
Citations number
69
Categorie Soggetti
Biochemistry & Biophysics
Journal title
FEBS LETTERS
ISSN journal
00145793 → ACNP
Volume
442
Issue
1
Year of publication
1999
Pages
1 - 6
Database
ISI
SICI code
0014-5793(19990108)442:1<1:HBCPAA>2.0.ZU;2-L
Abstract
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.