6533b873fe1ef96bd12d4e89
RESEARCH PRODUCT
Mosaic particles formed by wild-type hepatitis B virus core protein and its deletion variants consist of both homo- and heterodimers.
Andris DishlersDetlev H. KrügerRainer UlrichHelga MeiselAndris KazaksPaul Pumpenssubject
Hepatitis B virusvirusesProtein subunitDimerBiophysicsExpressionPlasma protein bindingBiologymedicine.disease_causeMosaic particlesBiochemistrychemistry.chemical_compoundHepatitis B virus core proteinProtein structureStructural Biologyparasitic diseasesGeneticsmedicineHepatitis B VaccinesCloning MolecularProtein Structure QuaternaryMolecular BiologyEscherichia coliSequence Deletionchemistry.chemical_classificationHepatitis B virusViral Core ProteinsWild typevirus diseasesGenetic VariationCell BiologyHepatitis BDimer formationVirologyMolecular biologydigestive system diseasesAmino acidProtein SubunitschemistryDimerizationProtein Bindingdescription
AbstractCo-expression in Escherichia coli of wild-type (wt) hepatitis B virus core protein (HBc) and its naturally occurring variants with deletions at amino acid positions 77–93 or 86–93 leads to formation of mosaic particles, which consist of three dimer subunit compositions. These compositions are wt/variant HBc heterodimers and two types of homodimers, formed by wt HBc or the variant HBc themselves. Mosaic particles were found also when both HBc deletion variants 77–93 and 86–93 were co-expressed in E. coli. These findings are discussed in terms of their significance for hepatitis B virus pathogenesis and prospective use of mosaic particles in vaccine development.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2003-07-25 | FEBS letters |