Evidence map›Paper›PMID 29535307›Full record

ArticleNature communications2018

Structure-based design of chimeric antigens for multivalent protein vaccines.

S Hollingshead, I Jongerius, R M Exley, S Johnson, S M Lea, C M Tang

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

20 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. PathogenicInfection and immunity · 2022
    Article
  7. Review
  8. Article
  9. Article
  10. Advances in vaccine delivery systems against viral infectious diseases.Drug delivery and translational research · 2021
    Review
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Structure-Based Vaccine Antigen Design.Annual review of medicine · 2019
    Review
  20. 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 2 institutions in 2 countries.

S HollingsheadSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford, OX1 3RE, UK.
I JongeriusSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford, OX1 3RE, UK.
R M ExleySir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford, OX1 3RE, UK.
S JohnsonSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford, OX1 3RE, UK.
S M LeaSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford, OX1 3RE, UK.ORCID http://orcid.org/0000-0001-9287-8053
C M TangSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford, OX1 3RE, UK. christoph.tang@path.ox.ac.uk.
University of Oxford · GBUniversity Medical Center Utrecht · NL

Funding

Medical Research Council G0900888Wellcome Trust 102908/Z/13/Z
6 · The paper itself

Abstract

There is an urgent need to develop vaccines against pathogenic bacteria. However, this is often hindered by antigenic diversity and difficulties encountered manufacturing membrane proteins. Here we show how to use structure-based design to develop chimeric antigens (ChAs) for subunit vaccines. ChAs are generated against serogroup B Neisseria meningitidis (MenB), the predominant cause of meningococcal disease in wealthy countries. MenB ChAs exploit factor H binding protein (fHbp) as a molecular scaffold to display the immunogenic VR2 epitope from the integral membrane protein PorA. Structural analyses demonstrate fHbp is correctly folded and the PorA VR2 epitope adopts an immunogenic conformation. In mice, immunisation with ChAs generates fHbp and PorA antibodies that recognise the antigens expressed by clinical MenB isolates; these antibody responses correlate with protection against meningococcal disease. Application of ChAs is therefore a potentially powerful approach to develop multivalent subunit vaccines, which can be tailored to circumvent pathogen diversity.

Indexed as

AnimalsAntibodies, BacterialAntigens, BacterialBacterial ProteinsHumansMeningococcal VaccinesNeisseria meningitidis, Serogroup BAntibodies, BacterialAntigens, BacterialBacterial ProteinsMeningococcal Vaccines

Identifiers

PMID29535307
PMCPMC5849709
OpenAlexW2893878597

What OpenQuestion holds

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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.