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

被引:99
作者
Pumpens, P [1 ]
Grens, E [1 ]
机构
[1] Latvian State Univ, Biomed Res & Study Ctr, LV-1067 Riga, Latvia
来源
FEBS LETTERS | 1999年 / 442卷 / 01期
关键词
hepatitis B core protein; self-assembly; protein structure; electron cryomicroscopy; molecular display; antigenicity;
D O I
10.1016/S0014-5793(98)01599-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Because it exhibits a remarkable capability to accept mutational intervention 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 foreign peptide sequences into several areas of HBc shells, including their most protruding spikes, Progress toward full resolution of the spatial structure as well as accumulation of chimeric HBc-based structures has brought closer the knowledge-based design of future vaccines, gene therapy tools and other artificial particulate objects. (C) 1999 Federation of European Biochemical Societies.
引用
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页码:1 / 6
页数:6
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