ArticleJournal of molecular biology2011
Role of the propeptide in controlling conformation and assembly state of hepatitis B virus e-antigen.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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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.
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Who cites it
19 citing papers in PubMed, 23 citations in OpenAlex.
- Hepatitis B Virus Nucleocapsid Assembly.Journal of molecular biology · 2025Review
- 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
- Probing the Hepatitis B Virus E-Antigen with a Nanopore Sensor Based on Collisional Events Analysis.Biosensors · 2022Article
- Amino acid residues at core protein dimer-dimer interface modulate multiple steps of hepatitis B virus replication and HBeAg biogenesis.PLoS pathogens · 2021Article
- Expression of quasi-equivalence and capsid dimorphism in the Hepadnaviridae.PLoS computational biology · 2020Article
- Capsids of hepatitis B virus e antigen with authentic C termini are stabilized by electrostatic interactions.FEBS letters · 2020Article
- Direct Inhibition of Hepatitis B e Antigen by Core Protein Allosteric Modulator.Hepatology (Baltimore, Md.) · 2019Article
- Structures of Hepatitis B Virus Core- and e-Antigen Immune Complexes Suggest Multi-point Inhibition.Structure (London, England : 1993) · 2018Article
- Novel Potent Capsid Assembly Modulators Regulate Multiple Steps of the Hepatitis B Virus Life Cycle.Antimicrobial agents and chemotherapy · 2018Article
- Chimeric rabbit/human Fab antibodies against the hepatitis Be-antigen and their potential applications in assays, characterization, and therapy.The Journal of biological chemistry · 2017Article
- The Structural Biology of Hepatitis B Virus: Form and Function.Annual review of virology · 2016Review
- Core protein: A pleiotropic keystone in the HBV lifecycle.Antiviral research · 2015Review
- Structurally similar woodchuck and human hepadnavirus core proteins have distinctly different temperature dependences of assembly.Journal of virology · 2014Article
- Assessment of differences in the conformational flexibility of hepatitis B virus core-antigen and e-antigen by hydrogen deuterium exchange-mass spectrometry.Protein science : a publication of the Protein Society · 2014Article
- Antigenic switching of hepatitis B virus by alternative dimerization of the capsid protein.Structure (London, England : 1993) · 2013Article
- One protein, at least three structures, and many functions.Structure (London, England : 1993) · 2013Article
- 3.5Å cryoEM structure of hepatitis B virus core assembled from full-length core protein.PloS one · 2013Article
- Hepatitis B precore protein: pathogenic potential and therapeutic promise.Yonsei medical journal · 2012Review
- Genome-wide networks of amino acid covariances are common among viruses.Journal of virology · 2012Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Hepatitis B virus "e-antigen" (HBeAg) is thought to be a soluble dimeric protein that is associated with chronic infection. It shares 149 residues with the viral capsid protein "core-antigen" (HBcAg), but has an additional 10-residue, hydrophobic, cysteine-containing amino-terminal propeptide whose presence correlates with physical, serological, and immunological differences between the two proteins. In HBcAg dimers, the subunits pair by forming a four-helix bundle stabilized by an intermolecular disulfide bond. The structure of HBeAg is probably similar but, instead, has two intramolecular disulfide bonds involving the propeptide. To compare the proteins directly and thereby clarify the role of the propeptide, we identified mutations and solution conditions that render both proteins as either soluble dimers or assembled capsids. Thermally induced unfolding monitored by circular dichroism, and electrophoresis of oxidized and reduced dimers, showed that the propeptide has a destabilizing effect and that the intramolecular disulfide bond forms preferentially and blocks the formation of the intermolecular disulfide bond that otherwise stabilizes the dimer. The HBeAg capsids are less regular than the HBcAg capsids; nevertheless, cryo-electron microscopy reconstructions confirm that they are constructed of dimers resembling those of HBcAg capsids. In them, a portion of the propeptide is visible near the dimer interface, suggesting that it intercalates there, consistent with the known formation of a disulfide bond between C(-7) in the propeptide and C61 in the dimer interface. However, this intercalation distorts the dimer into an assembly-reluctant conformation.
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Registered trials
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