Evidence map›Paper›PMID 25830365›Full record

ArticlePloS one2015

Tandem fusion of hepatitis B core antigen allows assembly of virus-like particles in bacteria and plants with enhanced capacity to accommodate foreign proteins.

Hadrien Peyret, Annick Gehin, Eva C Thuenemann, Donatienne Blond, Aadil El Turabi, Lucy Beales, Dean Clarke, Robert J C Gilbert, Elizabeth E Fry, David I Stuart and 6 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
11.8field-weighted citation impact, top 1% 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

63 citing papers in PubMed, 120 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. EngineeringVaccines · 2024
    Review
  7. Encapsulation of Transketolase intoACS applied bio materials · 2024
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Virus-like Particles for TEM Regulation and Antitumor Therapy.Journal of functional biomaterials · 2022
    Review
  15. Article
  16. Article
  17. Plant-Derived Human Vaccines: Recent Developments.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2022
    Review
  18. Review
  19. Review
  20. Review

3 more citing papers are in PubMed but not listed here.

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

16 authors at 5 institutions in 1 country.

Hadrien PeyretDepartment of Biological Chemistry, John Innes Centre, Norwich, United Kingdom.
Annick GehinSchool of Molecular and Cellular Biology, Faculty of Biological Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.
Eva C ThuenemannDepartment of Biological Chemistry, John Innes Centre, Norwich, United Kingdom.
Donatienne BlondSchool of Molecular and Cellular Biology, Faculty of Biological Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.
Aadil El TurabiSchool of Molecular and Cellular Biology, Faculty of Biological Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom; iQur Ltd, London, United Kingdom.
Lucy BealesSchool of Molecular and Cellular Biology, Faculty of Biological Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom; iQur Ltd, London, United Kingdom.
Dean ClarkeSchool of Molecular and Cellular Biology, Faculty of Biological Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.
Robert J C GilbertUK Division of Structural Biology, University of Oxford, Oxford, United Kingdom.
Elizabeth E FryUK Division of Structural Biology, University of Oxford, Oxford, United Kingdom.
David I StuartUK Division of Structural Biology, University of Oxford, Oxford, United Kingdom.
Kris HolmesSchool of Molecular and Cellular Biology, Faculty of Biological Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.
Nicola J StonehouseSchool of Molecular and Cellular Biology, Faculty of Biological Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.
Mike WhelaniQur Ltd, London, United Kingdom.
William RosenbergiQur Ltd, London, United Kingdom.
George P LomonossoffDepartment of Biological Chemistry, John Innes Centre, Norwich, United Kingdom.
David J RowlandsSchool of Molecular and Cellular Biology, Faculty of Biological Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.
Institute of Structural and Molecular Biology · GBiQur (United Kingdom) · GBJohn Innes Centre · GBUniversity of Oxford · GBUniversity of Leeds · GB

Funding

Biotechnology and Biological Sciences Research Council 24/SBD07645Biotechnology and Biological Sciences Research Council BB/J004596/1Biotechnology and Biological Sciences Research Council BBS/E/J/00000166Biotechnology and Biological Sciences Research Council BBS/E/J/000CA374Medical Research Council G1000099Wellcome TrustWellcome Trust 060208/Z/00/ZWellcome Trust 093305/Z/10/Z
6 · The paper itself

Abstract

The core protein of the hepatitis B virus, HBcAg, assembles into highly immunogenic virus-like particles (HBc VLPs) when expressed in a variety of heterologous systems. Specifically, the major insertion region (MIR) on the HBcAg protein allows the insertion of foreign sequences, which are then exposed on the tips of surface spike structures on the outside of the assembled particle. Here, we present a novel strategy which aids the display of whole proteins on the surface of HBc particles. This strategy, named tandem core, is based on the production of the HBcAg dimer as a single polypeptide chain by tandem fusion of two HBcAg open reading frames. This allows the insertion of large heterologous sequences in only one of the two MIRs in each spike, without compromising VLP formation. We present the use of tandem core technology in both plant and bacterial expression systems. The results show that tandem core particles can be produced with unmodified MIRs, or with one MIR in each tandem dimer modified to contain the entire sequence of GFP or of a camelid nanobody. Both inserted proteins are correctly folded and the nanobody fused to the surface of the tandem core particle (which we name tandibody) retains the ability to bind to its cognate antigen. This technology paves the way for the display of natively folded proteins on the surface of HBc particles either through direct fusion or through non-covalent attachment via a nanobody.

Indexed as

Protein MultimerizationVirusesArtificial Gene FusionEscherichia coliGreen Fluorescent ProteinsHepatitis B Core AntigensModels, MolecularNicotianaProtein Structure, QuaternarySingle-Domain AntibodiesGreen Fluorescent ProteinsHepatitis B Core AntigensSingle-Domain Antibodies

Identifiers

PMID25830365
PMCPMC4382129
OpenAlexW2003382316

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.