ArticleJournal of structural biology2012
Cryo-EM study of Hepatitis B virus core antigen capsids decorated with antibodies from a human patient.
Article in Journal of structural biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- The characterization and structural basis of a human broadly binding antibody to HBV core protein.Journal of virology · 2025Article
- Cryo EM structures map a post vaccination polyclonal antibody response to canine parvovirus.Communications biology · 2023Article
- Research advances in hydrogen-deuterium exchange mass spectrometry for protein epitope mapping.Analytical and bioanalytical chemistry · 2021Review
- Structural Basis of Human Parechovirus Neutralization by Human Monoclonal Antibodies.Journal of virology · 2015Article
- 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
- Epitope-distal effects accompany the binding of two distinct antibodies to hepatitis B virus capsids.Journal of the American Chemical Society · 2013Article
- Antigenic switching of hepatitis B virus by alternative dimerization of the capsid protein.Structure (London, England : 1993) · 2013Article
- Specificity of an anti-capsid antibody associated with Hepatitis B Virus-related acute liver failure.Journal of structural biology · 2013Article
- Fabs enable single particle cryoEM studies of small proteins.Structure (London, England : 1993) · 2012Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
The capsid (core antigen, HBcAg) is one of three major antigens present in patients infected with Hepatitis B virus. The capsids are icosahedral particles, whose most prominent features are spikes that extend 25 Å out from the contiguous "floor". At the spike tip are two copies of the "immunodominant loop". Previously, the epitopes of seven murine monoclonal antibodies have been identified by cryo-EM analysis of Fab-labeled capsids. All but one are conformational and all but one map around the spike tip. The exception, which is also the tightest-binder, straddles an inter-molecular interface on the floor. Seeking to relate these observations to the immunological response of infected humans, we isolated anti-cAg antibodies from a patient, prepared Fabs, and analyzed their binding to capsids. A priori, one possibility was that many different Fabs would give an undifferentiated continuum of Fab-related density. In fact, the density observed was highly differentiated and could be reproduced by modeling with just five Fabs, three binding to the spike and two to the floor. These results show that epitopes on the floor, far (~30 Å) from the immunodominant loop, are clinically relevant and that murine anti-cAg antibodies afford a good model for the human system.
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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.