6533b7dbfe1ef96bd126f772
RESEARCH PRODUCT
Hepatitis B core particles as a universal display model: a structure-function basis for development
Elmars GrensPaul Pumpenssubject
Hepatitis B virusGenes ViralCryo-electron microscopyMacromolecular SubstancesProtein ConformationBiophysicsComputational biologyBiologyBiochemistryMolecular displayEpitopesProtein structureStructural BiologyGeneticsProkaryotic expressionAnimalsHumansMolecular BiologyDrug CarriersBinding SitesSpatial structureViral Core ProteinsStructure functionHepatitis B core proteinvirus diseasesCell BiologyBasis (universal algebra)Self-assemblyAntigenicityVirologyBiological EvolutionHepatitis B Core Antigensdigestive system diseasesFolding (chemistry)Protein structureElectron cryomicroscopyDimerizationHepatitis b coredescription
AbstractBecause 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 α-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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1999-01-29 | FEBS Letters |