Evidence map›Paper›PMID 28290225›Full record

ReviewExpert review of vaccines2017

Influence of protein fold stability on immunogenicity and its implications for vaccine design.

Sandra Scheiblhofer, Josef Laimer, Yoan Machado, Richard Weiss, Josef Thalhamer

Abstract readReview
In one paragraph

Review in Expert review of vaccines, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 117 papers.

0numbers the graph read from it
0cells of the map it votes in
117citing papers in PubMed
–field-weighted citation impact
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

117 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Stabilized mosaic hemagglutinin immunogens as novel universal influenza virus vaccines.Molecular therapy : the journal of the American Society of Gene Therapy · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. CD207-Positive Dendritic Cells Promote Emphysema Through CD8Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  14. Article
  15. Mucosal vaccination with enzymatically activeFrontiers in microbiology · 2026
    Article
  16. Article
  17. Article
  18. Article
  19. Modulating antigen processing through metal-organic frameworks to bias adaptive immunity.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  20. Article

57 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

5 authors.

Sandra Scheiblhofera Department of Molecular Biology , University of Salzburg , Salzburg , Austria.
Josef Laimera Department of Molecular Biology , University of Salzburg , Salzburg , Austria.
Yoan Machadoa Department of Molecular Biology , University of Salzburg , Salzburg , Austria.
Richard Weissa Department of Molecular Biology , University of Salzburg , Salzburg , Austria.
Josef Thalhamera Department of Molecular Biology , University of Salzburg , Salzburg , Austria.

Funding

Austrian Science Fund FWF P 26997
6 · The paper itself

Abstract

introductionIn modern vaccinology and immunotherapy, recombinant proteins more and more replace whole organisms to induce protective or curative immune responses. Structural stability of proteins is of crucial importance for efficient presentation of antigenic peptides on MHC, which plays a decisive role for triggering strong immune reactions. Areas covered: In this review, we discuss structural stability as a key factor for modulating the potency of recombinant vaccines and its importance for antigen proteolysis, presentation, and stimulation of B and T cells. Moreover, the impact of fold stability on downstream events determining the differentiation of T cells into effector cells is reviewed. We summarize studies investigating the impact of protein fold stability on the outcome of the immune response and provide an overview on computational methods to estimate the effects of point mutations on protein stability. Expert commentary: Based on this information, the rational design of up-to-date vaccines is discussed. A model for predicting immunogenicity of proteins based on their conformational stability at different pH values is proposed.

Indexed as

AnimalsAntigensDisease Models, AnimalDrug DesignDrug StabilityHumansProtein FoldingRecombinant ProteinsVaccinesAntigensRecombinant ProteinsVaccinesconformational stabilitydestabilizationfold stabilityimmunogenicityprocessingProtein stabilityprotein variantsrecombinant vaccinesstabilization

Identifiers

PMID28290225
PMCPMC5490637

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.