Hepatitis B Virus Core Protein Domains Essential for Viral Capsid Assembly in a Cellular Context
نویسندگان
چکیده
منابع مشابه
Hepatitis B virus capsid assembly Assembly pathway of hepatitis B core virus-like particles from genetically fused dimers
Background: We studied assembly of HBV capsids using a genetically-fused dimer. Results: Assembly intermediates composed of two, three and five copies of a fused dimer have been isolated. Conclusion: Capsid assembly could progress using dimeric, trimeric and pentameric intermediates. Significance: The low abundance and transient nature of assembly intermediates make analysis challenging, howeve...
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The C-terminal domain (CTD) of Hepatitis B virus (HBV) core protein is involved in regulating multiple stages of the HBV lifecycle. CTD phosphorylation correlates with pregenomic-RNA encapsidation during capsid assembly, reverse transcription, and viral transport, although the mechanisms remain unknown. In vitro, purified HBV core protein (Cp183) binds any RNA and assembles aggressively, indepe...
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The HBV (hepatitis B virus) core is a phosphoprotein whose assembly, replication, encapsidation and localization are regulated by phosphorylation. It is known that PKC (protein kinase C) regulates pgRNA (pregenomic RNA) encapsidation by phosphorylation of the C-terminus of core, which is a component packaged into capsid. Neither the N-terminal residue phosphorylated by PKC nor the role of the C...
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UNLABELLED Multiple subunits of the hepatitis B virus (HBV) core protein (HBc) assemble into an icosahedral capsid that packages the viral pregenomic RNA (pgRNA). The N-terminal domain (NTD) of HBc is sufficient for capsid assembly, in the absence of pgRNA or any other viral or host factors, under conditions of high HBc and/or salt concentrations. The C-terminal domain (CTD) is deemed dispensab...
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ژورنال
عنوان ژورنال: Journal of Molecular Biology
سال: 2020
ISSN: 0022-2836
DOI: 10.1016/j.jmb.2020.04.026