Evidence map›Paper›PMID 23430249›Full record

ArticleThe Journal of biological chemistry2013

Natural HLA-B*2705 protein ligands with glutamine as anchor motif: implications for HLA-B27 association with spondyloarthropathy.

Susana Infantes, Elena Lorente, Eilon Barnea, Ilan Beer, Alejandro Barriga, Fátima Lasala, Mercedes Jiménez, Arie Admon, Daniel López

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

13 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. The Human Leukocyte Antigen (HLA)-B27 PeptidomeMolecular & cellular proteomics : MCP · 2017
    Article
  8. Article
  9. Article
  10. Revisiting MHC genes in spondyloarthritis.Current rheumatology reports · 2015
    Review
  11. Article
  12. Short peptide sequence identity between human viruses and HLA-B27-binding human 'self' peptides.Theory in biosciences = Theorie in den Biowissenschaften · 2014
    Article
  13. 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

9 authors at 4 institutions in 2 countries.

Susana InfantesCentro Nacional de Microbiología, Instituto de Salud Carlos III, 28220 Majadahonda (Madrid), Spain.
Elena Lorente
Eilon Barnea
Ilan Beer
Alejandro Barriga
Fátima Lasala
Mercedes Jiménez
Arie Admon
Daniel López
Instituto de Salud Carlos III · ESTechnion – Israel Institute of Technology · ILCentro Nacional de Microbiologia · ESIBM Research - Haifa · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The presentation of short viral peptide antigens by human leukocyte antigen (HLA) class I molecules on cell surfaces is a key step in the activation of cytotoxic T lymphocytes, which mediate the killing of pathogen-infected cells or initiate autoimmune tissue damage. HLA-B27 is a well known class I molecule that is used to study both facets of the cellular immune response. Using mass spectrometry analysis of complex HLA-bound peptide pools isolated from large amounts of HLA-B*2705(+) cells, we identified 200 naturally processed HLA-B*2705 ligands. Our analyses revealed that a change in the position (P) 2 anchor motif was detected in the 3% of HLA-B*2705 ligands identified. B*2705 class I molecules were able to bind these six GlnP2 peptides, which showed significant homology to pathogenic bacterial sequences, with a broad range of affinities. One of these ligands was able to bind with distinct conformations to HLA-B27 subtypes differentially associated with ankylosing spondylitis. These conformational differences could be sufficient to initiate autoimmune damage in patients with ankylosing spondylitis-associated subtypes. Therefore, these kinds of peptides (short, with GlnP2, and similar low affinity to all HLA-B27 subtypes tested but with unlike conformations in differentially ankylosing spondylitis-associated subtypes) must not be excluded from future researches involving potential arthritogenic peptides.

Indexed as

Amino Acid MotifsCell LineHLA-B27 AntigenHumansPeptidesProtein BindingSpondylarthropathiesHLA-B*27:05 antigenHLA-B27 AntigenPeptides

Identifiers

PMID23430249
PMCPMC3624468
OpenAlexW2154988908

What OpenQuestion holds

Textmetadata
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.