ArticleScientific reports2019
Direct interaction between the hepatitis B virus core and envelope proteins analyzed in a cellular context.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed, 39 citations in OpenAlex.
- Review
- Red Alga Porphyridium Supports High-Yield Production of a Functional Chimeric Hepatitis B Surface Antigen With Strong Cellular and Humoral Immunogenicity.Plant biotechnology journal · 2025Article
- Identification of low-molecular compounds that inhibit envelope formation of hepatitis B virus.Scientific reports · 2025Article
- Mutational landscape of the surface antigen of hepatitis B virus in patients with hepatocellular carcinoma.Gut pathogens · 2025Article
- The HBV large envelope protein initiates virion assembly by recruiting capsids at membrane rich domains related to late endosome.Cellular and molecular life sciences : CMLS · 2025Article
- Hepatitis B virus entry, assembly, and egress.Microbiology and molecular biology reviews : MMBR · 2024Review
- NEDD4 family ubiquitin ligase AIP4 interacts with Alix to enable HBV naked capsid egress in an Alix ubiquitination-independent manner.PLoS pathogens · 2024Article
- M133S mutation possibly involve in the ER stress and mitophagy pathway in maintenance hemodialysis patients with occult hepatitis B infection.Scientific reports · 2024Article
- Hepatitis B Surface Antigen Isoforms: Their Clinical Implications, Utilisation in Diagnosis, Prevention and New Antiviral Strategies.Pathogens (Basel, Switzerland) · 2024Review
- 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
- Conserved Lysine Residues of Hepatitis B Virus Core Protein Are Not Required for Covalently Closed Circular DNA Formation.Journal of virology · 2022Article
- Hepatitis B and circadian rhythm of the liver.World journal of gastroenterology · 2022Review
- Review
- Molecular Mechanisms during Hepatitis B Infection and the Effects of the Virus Variability.Viruses · 2021Review
- Envelope Proteins of Hepatitis B Virus: Molecular Biology and Involvement in Carcinogenesis.Viruses · 2021Review
- Regulation of Hepatitis B Virus Replication by Cyclin Docking Motifs in Core Protein.Journal of virology · 2021Article
- Conformational Plasticity of Hepatitis B Core Protein Spikes Promotes Peptide Binding Independent of the Secretion Phenotype.Microorganisms · 2021Article
- Hepatitis B Core Protein Capsids.Sub-cellular biochemistry · 2021Review
- Review
- Intracellular Trafficking of HBV Particles.Cells · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hepatitis B virus (HBV) production requires intricate interactions between the envelope and core proteins. Analyses of mutants of these proteins have made it possible to map regions involved in the formation and secretion of virions. Tests of binding between core and envelope peptides have also been performed in cell-free conditions, to study the interactions potentially underlying these mechanisms. We investigated the residues essential for core-envelope interaction in a cellular context in more detail, by transiently producing mutant or wild-type L, S, or core proteins separately or in combination, in Huh7 cells. The colocalization and interaction of these proteins were studied by confocal microscopy and co-immunoprecipitation, respectively. The L protein was shown to constitute a molecular platform for the recruitment of S and core proteins in a perinuclear environment. Several core amino acids were found to be essential for direct interaction with L, including residue Y132, known to be crucial for capsid formation, and residues L60, L95, K96 and I126. Our results confirm the key role of L in the tripartite core-S-L interaction and identify the residues involved in direct core-L interaction. This model may be valuable for studies of the potential of drugs to inhibit HBV core-envelope interaction.
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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.