Evidence map›Paper›PMID 22750730›Full record

ArticleJournal of molecular biology2012

Structures of hepatitis B virus cores presenting a model epitope and their complexes with antibodies.

A M Roseman, O Borschukova, J A Berriman, S A Wynne, P Pumpens, R A Crowther

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

19 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Synthesis and Assembly of Hepatitis B Virus-Like Particles in aFrontiers in bioengineering and biotechnology · 2020
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Immunopathogenesis of chronic hepatitis B.World journal of gastroenterology · 2014
    Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

A M RosemanMRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK. Alan.Roseman@manchester.ac.uk
O Borschukova
J A Berriman
S A Wynne
P Pumpens
R A Crowther
MRC Laboratory of Molecular Biology · GBLatvian Biomedical Research and Study Centre · LVUniversity of Manchester · GB

Funding

Medical Research Council MC_U105184322Medical Research Council U105184319
6 · The paper itself

Abstract

The core shell of hepatitis B virus is a potent immune stimulator, giving a strong neutralizing immune response to foreign epitopes inserted at the immunodominant region, located at the tips of spikes on the exterior of the shell. Here, we analyze structures of core shells with a model epitope inserted at two alternative positions in the immunodominant region. Recombinantly expressed core protein assembles into T=3 and T=4 icosahedral shells, and atomic coordinates are available for the T=4 shell. Since the modified protein assembles predominantly into T=3 shells, a quasi-atomic model of the native T=3 shell was made. The spikes in this T=3 structure resemble those in T=4 shells crystallized from expressed protein. However, the spikes in the modified shells exhibit an altered conformation, similar to the DNA containing shells in virions. Both constructs allow full access of antibodies to the foreign epitope, DPAFR from the preS1 region of hepatitis B virus surface antigen. However, one induces a 10-fold weaker immune response when injected into mice. In this construct, the epitope is less constrained by the flanking linker regions and is positioned so that the symmetry of the shell causes pairs of epitopes to come close enough to interfere with one another. In the other construct, the epitope mimics the native epitope conformation and position. The interaction of native core shells with an antibody specific to the immunodominant epitope is compared to the constructs with an antibody against the foreign epitope. Our findings have implications for the design of vaccines based on virus-like particles.

Indexed as

Amino Acid SequenceAnimalsAntigen-Antibody ComplexEpitopesHepatitis B AntibodiesHepatitis B Core AntigensHepatitis B Surface AntigensHepatitis B virusMiceMolecular Sequence DataProtein ConformationAntigen-Antibody ComplexEpitopesHepatitis B AntibodiesHepatitis B Core AntigensHepatitis B Surface Antigens

Identifiers

PMID22750730
PMCPMC3465560
OpenAlexW1978089216

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.