Journal of Virology · 1991 · 24 citations · 31 references
Life SciencesBiochemistryMolecular BiologyMolecular VirologyStructural BiologyVirologyDisulfide Bond FormationProtein StructureViral AssemblyViral HepatitisViral StructureVirus StructureDisulfide ChemistryDisulfide ContributionsPh DependenceSelf-assembly MechanismsViral Core StructureViral Hepatitis Pathogenesis
Our understanding of the assembly of hepatitis B virus is still very limited. We present evidence to demonstrate that the HBc antigen formed oligomers through disulfide linkages in the extracellular hepatitis B virus core (HBc) particles. However, the intracellular HBV core particles did not contain disulfide-linked HBc antigens. Furthermore, the extracellular particles which had disulfide bonds were more stable than intracellular particles at pH 7.5 and 10 and in 3 M NaCl and 4 M urea. These data suggest that the formation of disulfide bonds in the HBc antigen is important for the integrity of the viral core particles.
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