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

P Pumpens; E Grens

doi:10.1016/s0014-5793(98)01599-3

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

P Pumpens·E Grens

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Abstract

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.

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Animals Binding Sites Biological Evolution Dimerization Drug Carriers Epitopes Genes, Viral Hepatitis B Core Antigens Hepatitis B virus Humans Macromolecular Substances Protein Conformation Viral Core Proteins Journal Article Review

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P Pumpens, E Grens. 1999-01-08. Hepatitis B core particles as a universal display model: a structure-function basis for development.. https://doi.org/10.1016/s0014-5793(98)01599-3

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