Evidence map›Paper›PMID 30691364›Full record

ReviewAnnual review of medicine2019

Structure-Based Vaccine Antigen Design.

Barney S Graham, Morgan S A Gilman, Jason S McLellan

Open access · greenAbstract readReview
In one paragraph

Review in Annual review of medicine, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 158 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
158citing papers in PubMed, 1 pooled it
18.7field-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

158 citing papers in PubMed, 1 synthesis or guideline pooled it, 239 citations in OpenAlex.

  1. Controlling timing and location in vaccines.Advanced drug delivery reviews · 2020
    Pooled it
  2. Trial
  3. Trial
  4. Trial
  5. Trial
  6. Article
  7. In Vitro Selection of Antibodies TargetingPathogens (Basel, Switzerland) · 2026
    Article
  8. Global vaccine development.Nature medicine · 2026
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Immunofocusing design of a fusion glycoprotein monomer vaccine for respiratory syncytial virus.Molecular therapy : the journal of the American Society of Gene Therapy · 2025
    Article
  20. Article

98 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

3 authors at 2 institutions in 1 country.

Barney S GrahamVaccine Research Center, National Institute of Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20850, USA; email: bgraham@nih.gov.
Morgan S A GilmanDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, Texas 78712, USA; email: jmclellan@austin.utexas.edu.
Jason S McLellanDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, Texas 78712, USA; email: jmclellan@austin.utexas.edu.
The University of Texas at Austin · USNational Institutes of Health · US

Funding

Antigenicity and Immunogenicity of Stabilized prefusion F proteinZIAAI005129 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI GRAHAM, BARNEY · 2016 to 2021
$7.9M
Structure, Function and Antigenicity of Coronavirus Spike ProteinsR01AI127521 · NIAID · UNIVERSITY OF TEXAS AT AUSTIN · PI MCLELLAN, JASON SCOTT, WARD, ANDREW BARRETT · 2017 to 2021
$3.1M
NIAID NIH HHS R01 AI127521
6 · The paper itself

Abstract

Enabled by new approaches for rapid identification and selection of human monoclonal antibodies, atomic-level structural information for viral surface proteins, and capacity for precision engineering of protein immunogens and self-assembling nanoparticles, a new era of antigen design and display options has evolved. While HIV-1 vaccine development has been a driving force behind these technologies and concepts, clinical proof-of-concept for structure-based vaccine design may first be achieved for respiratory syncytial virus (RSV), where conformation-dependent access to neutralization-sensitive epitopes on the fusion glycoprotein determines the capacity to induce potent neutralizing activity. Success with RSV has motivated structure-based stabilization of other class I viral fusion proteins for use as immunogens and demonstrated the importance of structural information for developing vaccines against other viral pathogens, particularly difficult targets that have resisted prior vaccine development efforts. Solving viral surface protein structures also supports rapid vaccine antigen design and application of platform manufacturing approaches for emerging pathogens.

Indexed as

AnimalsAntibodies, MonoclonalAntibodies, NeutralizingB-LymphocytesHumansRespiratory Syncytial VirusesSensitivity and SpecificityStructure-Activity RelationshipVaccines, SyntheticViral Fusion ProteinsViral VaccinesAntibodies, MonoclonalAntibodies, NeutralizingVaccines, SyntheticViral Fusion ProteinsViral Vaccinescoronaviruselectron microscopyimmunizationinfluenzananoparticle displayplatform technologyrespiratory syncytial virusvaccine developmentX-ray crystallography

Identifiers

PMID30691364
PMCPMC6936610
OpenAlexW2913893387

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.