ArticleJournal of structural biology2013
Specificity of an anti-capsid antibody associated with Hepatitis B Virus-related acute liver failure.
Article in Journal of structural biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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.
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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
15 citing papers in PubMed, 21 citations in OpenAlex.
- Massive hepatic necrosis-associated acute liver failure.eGastroenterology · 2026Review
- Hepatitis B Core Protein Capsids.Sub-cellular biochemistry · 2021Review
- Assembly and Characterization of HBc Derived Virus-like Particles with Magnetic Core.Nanomaterials (Basel, Switzerland) · 2019Article
- Bioinformatic identification of key genes and pathways that may be involved in the pathogenesis of HBV-associated acute liver failure.Genes & diseases · 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
- Accurate model annotation of a near-atomic resolution cryo-EM map.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Zoonotic Hepatitis E Virus: An Ignored Risk for Public Health.Frontiers in microbiology · 2017Review
- Internal Proteins of the Procapsid and Mature Capsids of Herpes Simplex Virus 1 Mapped by Bubblegram Imaging.Journal of virology · 2016Article
- S-phase arrest after vincristine treatment may promote hepatitis B virus replication.World journal of gastroenterology · 2015Article
- 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
- Exploiting radiation damage to map proteins in nucleoprotein complexes: the internal structure of bacteriophage T7.Journal of structural biology · 2014Article
- Sizing up large protein complexes by electrospray ionisation-based electrophoretic mobility and native mass spectrometry: morphology selective binding of Fabs to hepatitis B virus capsids.Analytical and bioanalytical chemistry · 2014Article
- Development of Norwalk virus-specific monoclonal antibodies with therapeutic potential for the treatment of Norwalk virus gastroenteritis.Journal of virology · 2013Article
- Subunit folds and maturation pathway of a dsRNA virus capsid.Structure (London, England : 1993) · 2013Article
- Epitope-distal effects accompany the binding of two distinct antibodies to hepatitis B virus capsids.Journal of the American Chemical Society · 2013Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
Abstract
Previously, the livers of patients suffering from acute liver failure (ALF), a potentially fatal syndrome arising from infection by Hepatitis B Virus (HBV), were found to contain massive amounts of an antibody specific for the core antigen (HBcAg) capsid. We have used cryo-electron microscopy and molecular modeling to define its epitope. HBV capsids are icosahedral shells with 25Å-long dimeric spikes, each a 4-helix bundle, protruding from the contiguous "floor". Of the anti-HBcAg antibodies previously characterized, most bind around the spike tip while one binds to the floor. The ALF-associated antibody binds tangentially to a novel site on the side of the spike. This epitope is conformational. The Fab binds with high affinity to its principal determinants but has lower affinities for quasi-equivalent variants. The highest occupancy site is on one side of a spike, with no detectable binding to the corresponding site on the other side. Binding of one Fab per dimer was also observed by analytical ultracentrifugation. The Fab did not bind to the e-antigen dimer, a non-assembling variant of capsid protein. These findings support the propositions that antibodies with particular specificities may correlate with different clinical expressions of HBV infection and that antibodies directed to particular HBcAg epitopes may be involved in ALF pathogenesis.
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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.