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J Virol
1993 Jan 01;671:249-57. doi: 10.1128/JVI.67.1.249-257.1993.
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A micromolar pool of antigenically distinct precursors is required to initiate cooperative assembly of hepatitis B virus capsids in Xenopus oocytes.
Seifer M
,
Zhou S
,
Standring DN
.
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Assembly of hepatitis B virus capsid-like (core) particles occurs efficiently in a variety of heterologous systems via aggregation of approximately 180 molecules of a single 21.5-kDa core protein (p21.5), resulting in an icosahedral capsid structure with T = 3 symmetry. Recent studies on the assembly of hepatitis B virus core particles in Xenopus oocytes suggested that dimers of p21.5 represent the major building block from which capsids are generated. Here we determined the concentration dependence of this assembly process. By injecting serially diluted synthetic p21.5 mRNA into Xenopus oocytes, we expressed different levels of intracellular p21.5 and monitored the production of p21.5 dimers and capsids by radiolabeling and immunoprecipitation, by radioimmunoassay, or by quantitative enzyme-linked immunosorbent assay analysis. The data revealed that (i) p21.5 dimers and capsids are antigenically distinct, (ii) capsid assembly is a highly cooperative and concentration-dependent process, and (iii) p21.5 must accumulate to a signature concentration of approximately 0.7 to 0.8 microM before capsid assembly initiates. This assembly process is strikingly similar to the assembly of RNA bacteriophage R17 as defined by in vitro studies.
Almeida,
New antigen-antibody system in Australia-antigen-positive hepatitis.
1971, Pubmed
Almeida,
New antigen-antibody system in Australia-antigen-positive hepatitis.
1971,
Pubmed
Beckett,
Roles of operator and non-operator RNA sequences in bacteriophage R17 capsid assembly.
1988,
Pubmed
Beckett,
Ribonucleoprotein complexes of R17 coat protein and a translational operator analog.
1988,
Pubmed
Birnbaum,
Hepatitis B virus nucleocapsid assembly: primary structure requirements in the core protein.
1990,
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
Gurdon,
The use of Xenopus oocytes for the expression of cloned genes.
1983,
Pubmed
,
Xenbase
Hatton,
RNA- and DNA-binding activities in hepatitis B virus capsid protein: a model for their roles in viral replication.
1992,
Pubmed
,
Xenbase
Hogle,
Three-dimensional structure of poliovirus at 2.9 A resolution.
1985,
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
Luo,
The atomic structure of Mengo virus at 3.0 A resolution.
1987,
Pubmed
MacKay,
The conversion of hepatitis B core antigen synthesized in E coli into e antigen.
1981,
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
Magnius,
New specificities in Australia antigen positive sera distinct from the Le Bouvier determinants.
1972,
Pubmed
Ohori,
Antigenic conversion from HBcAg to HBeAg by degradation of hepatitis B core particles.
1980,
Pubmed
Ohori,
Immunological and morphological properties of HBeAg subtypes (HBeAg/1 and HBeAg/2) in hepatitis B virus core particles.
1984,
Pubmed
Onodera,
Electron microscopy of human hepatitis B virus cores by negative staining-carbon film technique.
1982,
Pubmed
Ou,
Hepatitis B virus gene function: the precore region targets the core antigen to cellular membranes and causes the secretion of the e antigen.
1986,
Pubmed
Rossmann,
Icosahedral RNA virus structure.
1989,
Pubmed
Stahl,
Immunogenicity of peptide fusions to hepatitis B virus core antigen.
1989,
Pubmed
Standring,
Assembly of viral particles in Xenopus oocytes: pre-surface-antigens regulate secretion of the hepatitis B viral surface envelope particle.
1986,
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
Takahashi,
Hepatitis B e antigen polypeptides isolated from sera of individuals infected with hepatitis B virus: comparison with HBeAg polypeptide derived from Dane particles.
1980,
Pubmed
Takahashi,
Immunochemical structure of hepatitis B e antigen in the serum.
1983,
Pubmed
Uy,
Precore sequence of hepatitis B virus inducing e antigen and membrane association of the viral core protein.
1986,
Pubmed
Witherell,
Specific interaction between RNA phage coat proteins and RNA.
1991,
Pubmed
Yamaguchi,
Cryo-electron microscopy of hepatitis B virus core particles produced by transformed yeast: comparison with negative staining and ultrathin sectioning.
1988,
Pubmed
Yang,
Hepatitis B virus p25 precore protein accumulates in Xenopus oocytes as an untranslocated phosphoprotein with an uncleaved signal peptide.
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,
Hepatitis B virus capsid particles are assembled from core-protein dimer precursors.
1992,
Pubmed
,
Xenbase