ArticleJournal of virology2010
Full-length hepatitis B virus core protein packages viral and heterologous RNA with similarly high levels of cooperativity.
Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
99 citing papers in PubMed, 156 citations in OpenAlex.
- Cryo-EM structures of HBV capsids from human cells at near-atomic resolution.Structure (London, England : 1993) · 2026Article
- Hepatitis B Virus Nucleocapsid Assembly.Journal of molecular biology · 2025Review
- Charge engineering controls cooperative assembly and loading in protein host-guest complexes.Journal of materials chemistry. B · 2025Article
- The HBV variant CpF97L supports the secretion of pgRNA-containing virions at a level much greater than WT HBV.Journal of virology · 2025Article
- Article
- HBc: the multifunctional architect of HBV replication, immune evasion, and therapeutic innovation.Frontiers in immunology · 2025Review
- Raman-based PAT for multi-attribute monitoring during VLP recovery by dual-stage CFF: attribute-specific spectral preprocessing for model transfer.Frontiers in bioengineering and biotechnology · 2025Article
- Identification of Host Proteins Involved in Hepatitis B Virus Genome Packaging.Journal of proteome research · 2024Article
- An HPLC-SEC-based rapid quantification method for vesicular stomatitis virus particles to facilitate process development.Molecular therapy. Methods & clinical development · 2024Article
- A nucleosome switch primes Hepatitis B Virus infection.bioRxiv : the preprint server for biology · 2024Article
- Introducing adjuvant-loaded particulate hepatitis B core antigen as an alternative therapeutic hepatitis B vaccine component.JHEP reports : innovation in hepatology · 2024Article
- Virus-like particles (VLPs): A promising platform for combating against Newcastle disease virus.Vaccine: X · 2024Review
- Raman-based PAT for VLP precipitation: systematic data diversification and preprocessing pipeline identification.Frontiers in bioengineering and biotechnology · 2024Article
- Effective removal of host cell-derived nucleic acids bound to hepatitis B core antigen virus-like particles by heparin chromatography.Frontiers in bioengineering and biotechnology · 2024Article
- Absolute Quantification of Hepatitis B Core Antigen (HBcAg) Virus-like Particles and Bound Nucleic Acids.Viruses · 2023Article
- Biology of the hepatitis B virus (HBV) core and capsid assembly modulators (CAMs) for chronic hepatitis B (CHB) cure.Global health & medicine · 2023Review
- Structural conservation of HBV-like capsid proteins over hundreds of millions of years despite the shift from non-enveloped to enveloped life-style.Nature communications · 2023Article
- Engineering Metastability into a Virus-like Particle to Enable Triggered Dissociation.Journal of the American Chemical Society · 2023Article
- Molecular elucidation of drug-induced abnormal assemblies of the hepatitis B virus capsid protein by solid-state NMR.Nature communications · 2023Article
- Size-selective downstream processing of virus particles and non-enveloped virus-like particles.Frontiers in bioengineering and biotechnology · 2023Review
39 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 5 institutions in 2 countries.
Funding
Abstract
A critical feature of a viral life cycle is the ability to selectively package the viral genome. In vivo, phosphorylated hepatitis B virus (HBV) core protein specifically encapsidates a complex of pregenomic RNA (pgRNA) and viral polymerase; it has been suggested that packaging is specific for the complex. Here, we test the hypothesis that core protein has intrinsic specificity for pgRNA, independent of the polymerase. For these studies, we also evaluated the effect of core protein phosphorylation on assembly and RNA binding, using phosphorylated core protein and a phosphorylation mimic in which S155, S162, and S170 were mutated to glutamic acid. We have developed an in vitro system where capsids are disassembled and assembly-active core protein dimer is purified. With this protein, we have reassembled empty capsids and RNA-filled capsids. We found that core protein dimer bound and encapsidated both the HBV pregenomic RNA and heterologous RNA with high levels of cooperativity, irrespective of phosphorylation. In direct competition assays, no specificity for pregenomic RNA was observed. This suggests that another factor, such as the viral polymerase, is required for specific packaging. These results also beg the question of what prevents HBV core protein from assembling on nonviral RNA, preserving the protein for virus production.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.