ArticlePLoS pathogens2012
Structural organization of pregenomic RNA and the carboxy-terminal domain of the capsid protein of hepatitis B virus.
Article in PLoS pathogens, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed.
- Immunogenicity of SARS-CoV-2 vaccine prototype based on virus-like particles of hepatitis B core antigen from genotype G and interleukin 12 expressing Semliki Forest virus as a genetic adjuvant.The Journal of general virology · 2026Article
- Structural organization of HBV pgRNA genome driven by phase separation in capsid confinement.Nature communications · 2026Article
- Cryo-EM structures of HBV capsids from human cells at near-atomic resolution.Structure (London, England : 1993) · 2026Article
- DNA synthesis inside the hepatitis B virus creates a high-energy spool.bioRxiv : the preprint server for biology · 2026Article
- HBV polymerase recruits the phosphatase PP1 to dephosphorylate HBc-Ser170 to complete encapsidation.PLoS pathogens · 2025Article
- Introducing adjuvant-loaded particulate hepatitis B core antigen as an alternative therapeutic hepatitis B vaccine component.JHEP reports : innovation in hepatology · 2024Article
- Review
- Transient RNA Interactions Leave a Covalent Imprint on a Viral Capsid Protein.Journal of the American Chemical Society · 2022Article
- Core Protein-Directed Antivirals and Importin β Can Synergistically Disrupt Hepatitis B Virus Capsids.Journal of virology · 2022Article
- Virus self-assembly proceeds through contact-rich energy minima.Science advances · 2021Article
- Early Steps of Hepatitis B Life Cycle: From Capsid Nuclear Import to cccDNA Formation.Viruses · 2021Review
- The HBV Core Protein and Core Particle Both Bind to the PPiase Par14 and Par17 to Enhance Their Stabilities and HBV Replication.Frontiers in microbiology · 2021Article
- Review
- Hepatitis B virus core protein phosphorylation: Identification of the SRPK1 target sites and impact of their occupancy on RNA binding and capsid structure.PLoS pathogens · 2018Article
- Common and Distinct Capsid and Surface Protein Requirements for Secretion of Complete and Genome-Free Hepatitis B Virions.Journal of virology · 2018Article
- Curating viscoelastic properties of icosahedral viruses, virus-based nanomaterials, and protein cages.Journal of biological physics · 2018Article
- Asymmetric Modification of Hepatitis B Virus (HBV) Genomes by an Endogenous Cytidine Deaminase inside HBV Cores Informs a Model of Reverse Transcription.Journal of virology · 2018Article
- Article
- Enhanced stability of a chimeric hepatitis B core antigen virus-like-particle (HBcAg-VLP) by a C-terminal linker-hexahistidine-peptide.Journal of nanobiotechnology · 2018Article
- MicroRNA-125b-5p mediates post-transcriptional regulation of hepatitis B virus replication via the LIN28B/let-7 axis.RNA biology · 2017Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The Hepatitis B Virus (HBV) double-stranded DNA genome is reverse transcribed from its RNA pregenome (pgRNA) within the virus core (or capsid). Phosphorylation of the arginine-rich carboxy-terminal domain (CTD) of the HBV capsid protein (Cp183) is essential for pgRNA encapsidation and reverse transcription. However, the structure of the CTD remains poorly defined. Here we report sub-nanometer resolution cryo-EM structures of in vitro assembled empty and pgRNA-filled Cp183 capsids in unphosphorylated and phosphorylation-mimic states. In empty capsids, we found unexpected evidence of surface accessible CTD density partially occluding pores in the capsid surface. We also observed that CTD organization changed substantively as a function of phosphorylation. In RNA-filled capsids, unphosphorylated CTDs favored thick ropes of RNA, while the phosphorylation-mimic favored a mesh of thin, high-density strands suggestive of single stranded RNA. These results demonstrate that the CTD can regulate nucleic acid structure, supporting the hypothesis that the HBV capsid has a functional role as a nucleic acid chaperone.
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