Click here to close
Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly.
We suggest using a current version of Chrome,
FireFox, or Safari.
A protease-sensitive hinge linking the two domains of the hepatitis B virus core protein is exposed on the viral capsid surface.
Seifer M
,
Standring DN
.
???displayArticle.abstract???
Core particles of hepatitis B virus are assembled from dimers of a single 185-residue (subtype adw) viral capsid or core protein (p21.5) which possesses two distinct domains: residues 1 to 144 form a minimal capsid assembly domain, and the arginine-rich, carboxyl-terminal residues 150 to 185 form a protamine-like domain that mediates nucleic acid binding. Little is known about the topography of the p21.5 polypeptide within either the p21.5 capsids or dimers. Here, using site-specific proteases and monoclonal antibodies, we have defined the accessibility of p21.5 residues in dimers and capsids assembled from wild-type and mutant hepatitis B virus core proteins in Xenopus oocytes and in vitro. The data reveal the protamine region to be accessible to external reagents in p21.5 dimers but largely cryptic in wild-type capsids. Strikingly, in capsids the only protease target region was a 9-residue peptide covering p21.5 residues Glu-145 to Asp-153, which falls largely between the two core protein domains. By analogy with protease-sensitive interdomain regions in other proteins, we propose that this peptide constitutes a hinge between the assembly and nucleic acid binding domains of p21.5. We further found that deletion or replacement of the terminal Cys-185 residue greatly increased surface exposure of the protamine tails in capsids, suggesting that a known disulfide linkage involving this residue tethers the protamine region inside the core particles. We propose that disruption of this disulfide linkage allows the protamine region to appear transiently on the surface of the core particle.
Argos,
A model for the hepatitis B virus core protein: prediction of antigenic sites and relationship to RNA virus capsid proteins.
1988, Pubmed
Argos,
A model for the hepatitis B virus core protein: prediction of antigenic sites and relationship to RNA virus capsid proteins.
1988,
Pubmed
Bichko,
Epitopes recognized by antibodies to denatured core protein of hepatitis B virus.
1993,
Pubmed
Birnbaum,
Hepatitis B virus nucleocapsid assembly: primary structure requirements in the core protein.
1990,
Pubmed
Clarke,
Presentation and immunogenicity of viral epitopes on the surface of hybrid hepatitis B virus core particles produced in bacteria.
1990,
Pubmed
Davies,
Structural basis of antibody function.
1983,
Pubmed
Edman,
Synthesis of hepatitis B surface and core antigens in E. coli.
1981,
Pubmed
Gallina,
A recombinant hepatitis B core antigen polypeptide with the protamine-like domain deleted self-assembles into capsid particles but fails to bind nucleic acids.
1989,
Pubmed
Ganem,
Assembly of hepadnaviral virions and subviral particles.
1991,
Pubmed
Godley,
Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity.
1992,
Pubmed
Hatton,
RNA- and DNA-binding activities in hepatitis B virus capsid protein: a model for their roles in viral replication.
1992,
Pubmed
,
Xenbase
Imai,
Demonstration of two distinct antigenic determinants on hepatitis B e antigen by monoclonal antibodies.
1982,
Pubmed
Kniskern,
Unusually high-level expression of a foreign gene (hepatitis B virus core antigen) in Saccharomyces cerevisiae.
1986,
Pubmed
Lanford,
Expression of hepatitis B virus core and precore antigens in insect cells and characterization of a core-associated kinase activity.
1990,
Pubmed
Machida,
Antigenic sites on the arginine-rich carboxyl-terminal domain of the capsid protein of hepatitis B virus distinct from hepatitis B core or e antigen.
1989,
Pubmed
Machida,
Phosphorylation in the carboxyl-terminal domain of the capsid protein of hepatitis B virus: evaluation with a monoclonal antibody.
1991,
Pubmed
Nassal,
The arginine-rich domain of the hepatitis B virus core protein is required for pregenome encapsidation and productive viral positive-strand DNA synthesis but not for virus assembly.
1992,
Pubmed
Nassal,
Topological analysis of the hepatitis B virus core particle by cysteine-cysteine cross-linking.
1992,
Pubmed
Pugh,
Characterization of the major duck hepatitis B virus core particle protein.
1989,
Pubmed
Salfeld,
Antigenic determinants and functional domains in core antigen and e antigen from hepatitis B virus.
1989,
Pubmed
Schlicht,
The duck hepatitis B virus core protein contains a highly phosphorylated C terminus that is essential for replication but not for RNA packaging.
1989,
Pubmed
Schödel,
The position of heterologous epitopes inserted in hepatitis B virus core particles determines their immunogenicity.
1992,
Pubmed
Seifer,
Expression pattern of the hepatitis B virus genome in transfected mouse fibroblasts.
1990,
Pubmed
Seifer,
A micromolar pool of antigenically distinct precursors is required to initiate cooperative assembly of hepatitis B virus capsids in Xenopus oocytes.
1993,
Pubmed
,
Xenbase
Seifer,
Stability governs the apparent expression of "particulate" hepatitis B e antigen by mutant hepatitis B virus core particles.
1993,
Pubmed
,
Xenbase
Standring,
A signal peptide encoded within the precore region of hepatitis B virus directs the secretion of a heterogeneous population of e antigens in Xenopus oocytes.
1988,
Pubmed
,
Xenbase
Sällberg,
Characterisation of a linear binding site for a monoclonal antibody to hepatitis B core antigen.
1991,
Pubmed
Takahashi,
Immunochemical structure of hepatitis B e antigen in the serum.
1983,
Pubmed
Zheng,
The structure of hepadnaviral core antigens. Identification of free thiols and determination of the disulfide bonding pattern.
1992,
Pubmed
Zhou,
Hepatitis B virus capsid particles are assembled from core-protein dimer precursors.
1992,
Pubmed
,
Xenbase
Zhou,
Production of hepatitis B virus nucleocapsidlike core particles in Xenopus oocytes: assembly occurs mainly in the cytoplasm and does not require the nucleus.
1991,
Pubmed
,
Xenbase
Zhou,
Characterization of hepatitis B virus capsid particle assembly in Xenopus oocytes.
1992,
Pubmed
,
Xenbase
Zhou,
Cys residues of the hepatitis B virus capsid protein are not essential for the assembly of viral core particles but can influence their stability.
1992,
Pubmed
,
Xenbase