Evidence map›Paper›PMID 30100358›Full record

ArticleStructure (London, England : 1993)2018

Structures of Hepatitis B Virus Core- and e-Antigen Immune Complexes Suggest Multi-point Inhibition.

Elif Eren, Norman R Watts, Altaira D Dearborn, Ira W Palmer, Joshua D Kaufman, Alasdair C Steven, Paul T Wingfield

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.3field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Hepatitis B Virus Nucleocapsid Assembly.Journal of molecular biology · 2025
    Review
  2. Review
  3. Article
  4. SARS-CoV-2 Spike Protein Interaction Space.International journal of molecular sciences · 2023
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Retrained Generic Antibodies Can Recognize SARS-CoV-2.The journal of physical chemistry letters · 2021
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Virus Assembly Antagonists from Redesigned Antibodies.Structure (London, England : 1993) · 2018
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 1 country.

Elif ErenLaboratory of Structural Biology Research, NIAMS, National Institutes of Health, Bethesda, MD 20892, USA.
Norman R WattsProtein Expression Laboratory, NIAMS, National Institutes of Health, Bethesda, MD 20892, USA.
Altaira D DearbornProtein Expression Laboratory, NIAMS, National Institutes of Health, Bethesda, MD 20892, USA.
Ira W PalmerProtein Expression Laboratory, NIAMS, National Institutes of Health, Bethesda, MD 20892, USA.
Joshua D KaufmanProtein Expression Laboratory, NIAMS, National Institutes of Health, Bethesda, MD 20892, USA.
Alasdair C StevenLaboratory of Structural Biology Research, NIAMS, National Institutes of Health, Bethesda, MD 20892, USA.
Paul T WingfieldProtein Expression Laboratory, NIAMS, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: wingfiep@mail.nih.gov.
National Institute of Arthritis and Musculoskeletal and Skin Diseases · USNational Institutes of Health · USProtein Express (United States) · US

Funding

Structural Biology Of Virus AssemblyZIAAR027002 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI WINGFIELD, PAUL T · 2009 to 2024
$19.2M
Production Of HIV And HIV Related Proteins For Structural StudiesZIAAR041115 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI WINGFIELD, PAUL T · 2009 to 2025
$16.9M
RECOMBINANT DNA PRODUCED HIV PROTEINS--PURIFICATION/STRUCTURAL CHARACTERZ01AR041115 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI WINGFIELD, PAUL T · 1996 to 2008
$889k
Intramural NIH HHS Z01 AR041115
6 · The paper itself

Abstract

Hepatitis B virus (HBV) is the leading cause of liver disease worldwide. While an adequate vaccine is available, current treatment options are limited, not highly effective, and associated with adverse effects, encouraging the development of alternative therapeutics. The HBV core gene encodes two different proteins: core, which forms the viral nucleocapsid, and pre-core, which serves as an immune modulator with multiple points of action. The two proteins mostly have the same sequence, although they differ at their N and C termini and in their dimeric arrangements. Previously, we engineered two human-framework antibody fragments (Fab/scFv) with nano- to picomolar affinities for both proteins. Here, by means of X-ray crystallography, analytical ultracentrifugation, and electron microscopy, we demonstrate that the antibodies have non-overlapping epitopes and effectively block biologically important assemblies of both proteins. These properties, together with the anticipated high tolerability and long half-lives of the antibodies, make them promising therapeutics.

Indexed as

AnimalsAntibodies, MonoclonalAntibodies, ViralBinding SitesCrystallography, X-RayHepatitis B Core AntigensHepatitis B e AntigensHepatitis B virusHumansMicroscopy, ElectronModels, MolecularProtein BindingProtein Structure, QuaternaryUltracentrifugationAntibodies, MonoclonalAntibodies, ViralHepatitis B Core AntigensHepatitis B e Antigensantibody fragmentscapsid assemblyepitopesFabHBcAgHBeAghepatitis B virusnucleocapsidscFvtherapeutics

Identifiers

PMID30100358
PMCPMC6170708
OpenAlexW2886355406

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.