Evidence map›Paper›PMID 18713974›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2008

Immunodominance of CD4 T cells to foreign antigens is peptide intrinsic and independent of molecular context: implications for vaccine design.

Jason M Weaver, Christopher A Lazarski, Katherine A Richards, Francisco A Chaves, Scott A Jenks, Paula R Menges, Andrea J Sant

Open access · bronzeAbstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

26 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Review
  3. Current medicinal chemistry · 2024
    Review
  4. Article
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  6. Cancer research communications · 2021
    Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Protein Vaccination Directs the CD4Journal of virology · 2019
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

7 authors at 1 institution in 1 country.

Jason M WeaverDavid H. Smith Center for Vaccine Biology and Immunology, AaB Institute of Biomedical Sciences, Department of Microbiology and Immunology, University of Rochester, Rochester, NY 14642, USA.
Christopher A Lazarski
Katherine A Richards
Francisco A Chaves
Scott A Jenks
Paula R Menges
Andrea J Sant
University of Rochester · US

Funding

Immunodominance in CD4 T Cell ResponsesR01AI051542 · NIAID · UNIVERSITY OF ROCHESTER · PI SANT, ANDREA JANINE · 2002 to 2012
$3.6M
NIAID NIH HHS HHSN266200700008CNIAID NIH HHS R01 AI051542NIAID NIH HHS R01AI51542PHS HHS HHSN 266200700008C
6 · The paper itself

Abstract

Immunodominance refers to the restricted peptide specificity of T cells that are detectable after an adaptive immune response. For CD4 T cells, many of the mechanisms used to explain this selectivity suggest that events related to Ag processing play a major role in determining a peptide's ability to recruit CD4 T cells. Implicit in these models is the prediction that the molecular context in which an antigenic peptide is contained will impact significantly on its immunodominance. In this study, we present evidence that the selectivity of CD4 T cell responses to peptides contained within protein Ags is not detectably influenced by the location of the peptide in a given protein or the primary sequence of the protein that bears the test peptide. We have used molecular approaches to change the location of peptides within complex protein Ags and to change the flanking sequences that border the peptide epitope to now include a protease site, and find that immunodominance or crypticity of a peptide observed in its native protein context is preserved. Collectively, these results suggest immunodominance of peptides contained in complex Ags is due to an intrinsic factor of the peptide, based upon the affinity of that peptide for MHC class II molecules. These findings are discussed with regard to implications for vaccine design.

Indexed as

VaccinesAnimalsCD4-Positive T-LymphocytesEpitopesHistocompatibility Antigens Class IIIsoantigensMiceMice, Inbred BALB CPeptide FragmentsPeptidesProteinsT-Cell Antigen Receptor SpecificityEpitopesHistocompatibility Antigens Class IIIsoantigensPeptide FragmentsPeptidesProteinsVaccines

Identifiers

PMID18713974
PMCPMC2814425
OpenAlexW1848613573

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.