Evidence map›Paper›PMID 23109910›Full record

ArticlePLoS biology2012

The molecular basis for recognition of CD1d/α-galactosylceramide by a human non-Vα24 T cell receptor.

Jacinto López-Sagaseta, Jennifer E Kung, Paul B Savage, Jenny Gumperz, Erin J Adams

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

19 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Structural plasticity in I-AFrontiers in immunology · 2022
    Article
  5. Review
  6. Article
  7. Novel Molecular Insights into Human Lipid-Mediated T Cell Immunity.International journal of molecular sciences · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. The CD1 size problem: lipid antigens, ligands, and scaffolds.Cellular and molecular life sciences : CMLS · 2014
    Review
  16. Article
  17. MAIT recognition of a stimulatory bacterial antigen bound to MR1.Journal of immunology (Baltimore, Md. : 1950) · 2013
    Article
  18. Review
  19. 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

5 authors at 3 institutions in 1 country.

Jacinto López-SagasetaDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, United States of America.
Jennifer E Kung
Paul B Savage
Jenny Gumperz
Erin J Adams
University of Chicago · USBrigham Young University · USUniversity of Wisconsin–Madison · US

Funding

Molecular Recognition of Ligand by the Gamma Delta T Cell ReceptorR01AI073922 · NIAID · UNIVERSITY OF CHICAGO · PI ADAMS, ERIN JUNE · 2007 to 2016
$3.8M
Analysis of Human NKT cell auto-antigensR01AI074940 · NIAID · UNIVERSITY OF WISCONSIN-MADISON · PI GUMPERZ, JENNY E. · 2009 to 2013
$1.8M
Structural determinants of CD1d-restricted TCR functionR01AI060777 · NIAID · UNIVERSITY OF WISCONSIN-MADISON · PI GUMPERZ, JENNY E. · 2004 to 2008
$1.4M
NIAID NIH HHS R01 AI060777NIAID NIH HHS R01 AI073922NIAID NIH HHS R01AI073922NIAID NIH HHS R01 AI074940
6 · The paper itself

Abstract

CD1d-mediated presentation of glycolipid antigens to T cells is capable of initiating powerful immune responses that can have a beneficial impact on many diseases. Molecular analyses have recently detailed the lipid antigen recognition strategies utilized by the invariant Vα24-Jα18 TCR rearrangements of iNKT cells, which comprise a subset of the human CD1d-restricted T cell population. In contrast, little is known about how lipid antigens are recognized by functionally distinct CD1d-restricted T cells bearing different TCRα chain rearrangements. Here we present crystallographic and biophysical analyses of α-galactosylceramide (α-GalCer) recognition by a human CD1d-restricted TCR that utilizes a Vα3.1-Jα18 rearrangement and displays a more restricted specificity for α-linked glycolipids than that of iNKT TCRs. Despite having sequence divergence in the CDR1α and CDR2α loops, this TCR employs a convergent recognition strategy to engage CD1d/αGalCer, with a binding affinity (∼2 µM) almost identical to that of an iNKT TCR used in this study. The CDR3α loop, similar in sequence to iNKT-TCRs, engages CD1d/αGalCer in a similar position as that seen with iNKT-TCRs, however fewer actual contacts are made. Instead, the CDR1α loop contributes important contacts to CD1d/αGalCer, with an emphasis on the 4'OH of the galactose headgroup. This is consistent with the inability of Vα24- T cells to respond to α-glucosylceramide, which differs from αGalCer in the position of the 4'OH. These data illustrate how fine specificity for a lipid containing α-linked galactose is achieved by a TCR structurally distinct from that of iNKT cells.

Indexed as

Amino Acid SequenceAntigen PresentationAntigens, CD1dbeta 2-MicroglobulinBinding SitesCrystallography, X-RayGalactosylceramidesHumansMolecular Sequence DataNatural Killer T-CellsReceptors, Antigen, T-Cellalpha-galactosylceramideAntigens, CD1dbeta 2-MicroglobulinCD1D protein, humanGalactosylceramidesReceptors, Antigen, T-CellValpha24 protein, human

Identifiers

PMID23109910
PMCPMC3479090
OpenAlexW2075843525

What OpenQuestion holds

Textmetadata
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.