ArticleJournal of virology2004
Hepatitis B virus capsid assembly is enhanced by naturally occurring mutation F97L.
Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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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
44 citing papers in PubMed.
- Modular Virus-like Particles for Antigen Presentation: Comparing Genetic Fusion and Click-Chemistry for Purification.International journal of molecular sciences · 2025Article
- The HBV variant CpF97L supports the secretion of pgRNA-containing virions at a level much greater than WT HBV.Journal of virology · 2025Article
- HBc: the multifunctional architect of HBV replication, immune evasion, and therapeutic innovation.Frontiers in immunology · 2025Review
- Fluorescence, Circular Dichroism and Mass Spectrometry as Tools to Study Virus Structure.Sub-cellular biochemistry · 2024Review
- Hepatitis B virus virion secretion is a CRM1-spike-mediated late event.Journal of biomedical science · 2022Article
- Article
- Review
- The Integrity of the Intradimer Interface of the Hepatitis B Virus Capsid Protein Dimer Regulates Capsid Self-Assembly.ACS chemical biology · 2020Article
- Targeting the multifunctional HBV core protein as a potential cure for chronic hepatitis B.Antiviral research · 2020Review
- Persistence of Hepatitis B Virus DNA and the Tempos between Virion Secretion and Genome Maturation in a Mouse Model.Journal of virology · 2019Article
- Discovery of Novel Hepatitis B Virus Nucleocapsid Assembly Inhibitors.ACS infectious diseases · 2019Article
- Naturally occurring core protein mutations compensate for the reduced replication fitness of a lamivudine-resistant HBV isolate.Antiviral research · 2019Article
- 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
- Structures of Hepatitis B Virus Core- and e-Antigen Immune Complexes Suggest Multi-point Inhibition.Structure (London, England : 1993) · 2018Article
- Article
- Hepatitis B virus core protein allosteric modulators can distort and disrupt intact capsids.eLife · 2018Article
- Discovery and Mechanistic Study of Benzamide Derivatives That Modulate Hepatitis B Virus Capsid Assembly.Journal of virology · 2017Article
- Hepatitis B virus core antigen mutations predict post-operative prognosis of patients with primary hepatocellular carcinoma.The Journal of general virology · 2017Article
- Allosteric Control of Icosahedral Capsid Assembly.The journal of physical chemistry. B · 2016Article
- Precore/core region mutations of hepatitis B virus related to clinical severity.World journal of gastroenterology · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In chronic hepatitis B virus (HBV) infections, one of the most common mutations to the virus occurs at amino acid 97 of the core protein, where leucine replaces either phenylalanine or isoleucine, depending on strain. This mutation correlates with changes in viral nucleic acid metabolism and/or secretion. We hypothesize that this phenotype is due in part to altered core assembly, a process required for DNA synthesis. We examined in vitro assembly of empty HBV capsids from wild-type and F97L core protein assembly domains. The mutation enhanced both the rate and extent of assembly relative to those for the wild-type protein. The difference between the two proteins was most obvious in the temperature dependence of assembly, which was dramatically stronger for the mutant protein, indicating a much more positive enthalpy. Since the structures of the mutant and wild-type capsids are essentially the same and the mutation is not involved in the contact between dimers, we suggest that the F97L mutation affects the dynamic behavior of dimer and capsid.
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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.