Evidence map›Paper›PMID 16505140›Full record

ArticleThe Journal of experimental medicine2006

A structural basis for selection and cross-species reactivity of the semi-invariant NKT cell receptor in CD1d/glycolipid recognition.

Lars Kjer-Nielsen, Natalie A Borg, Daniel G Pellicci, Travis Beddoe, Lyudmila Kostenko, Craig S Clements, Nicholas A Williamson, Mark J Smyth, Gurdyal S Besra, Hugh H Reid and 4 more

Abstract read
In one paragraph

Article in The Journal of experimental medicine, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing 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

62 citing papers in PubMed.

  1. Article
  2. Three-Dimensional Modeling ofAntibodies (Basel, Switzerland) · 2025
    Article
  3. Sensing mycobacteria through unconventional pathways.The Journal of clinical investigation · 2025
    Article
  4. Review
  5. Article
  6. Markers and makers of NKT17 cells.Experimental & molecular medicine · 2023
    Review
  7. Article
  8. Article
  9. Benzofuran sulfonates and small self-lipid antigens activate type II NKT cells via CD1d.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Article
  11. In Vivo Cytotoxicity by α-GalCer-transactivated NK Cells.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  12. Article
  13. Immune profiling of pediatric solid tumors.The Journal of clinical investigation · 2020
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review

2 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

14 authors.

Lars Kjer-NielsenDepartment of Microbiology and Immunology, University of Melbourne, Parkville, Victoria 3010, Australia.
Natalie A Borg
Daniel G Pellicci
Travis Beddoe
Lyudmila Kostenko
Craig S Clements
Nicholas A Williamson
Mark J Smyth
Gurdyal S Besra
Hugh H Reid
Mandvi Bharadwaj
Dale I Godfrey
Jamie Rossjohn
James McCluskey

Funding

Medical Research Council G0400421Medical Research Council G9901077Wellcome TrustWellcome Trust 072021/Z/03/Z
6 · The paper itself

Abstract

Little is known regarding the basis for selection of the semi-invariant alphabeta T cell receptor (TCR) expressed by natural killer T (NKT) cells or how this mediates recognition of CD1d-glycolipid complexes. We have determined the structures of two human NKT TCRs that differ in their CDR3beta composition and length. Both TCRs contain a conserved, positively charged pocket at the ligand interface that is lined by residues from the invariant TCR alpha- and semi-invariant beta-chains. The cavity is centrally located and ideally suited to interact with the exposed glycosyl head group of glycolipid antigens. Sequences common to mouse and human invariant NKT TCRs reveal a contiguous conserved "hot spot" that provides a basis for the reactivity of NKT cells across species. Structural and functional data suggest that the CDR3beta loop provides a plasticity mechanism that accommodates recognition of a variety of glycolipid antigens presented by CD1d. We propose a model of NKT TCR-CD1d-glycolipid interaction in which the invariant CDR3alpha loop is predicted to play a major role in determining the inherent bias toward CD1d. The findings define a structural basis for the selection of the semi-invariant alphabeta TCR and the unique antigen specificity of NKT cells.

Indexed as

AnimalsAntigen PresentationAntigens, CD1Genes, T-Cell Receptor alphaGenes, T-Cell Receptor betaGlycolipidsHumansKiller Cells, NaturalMiceProtein BindingProtein Structure, QuaternaryProtein Structure, TertiaryReceptors, Antigen, T-Cell, alpha-betaSpecies SpecificityStructural Homology, ProteinStructure-Activity RelationshipAntigens, CD1GlycolipidsReceptors, Antigen, T-Cell, alpha-beta

Identifiers

PMID16505140
PMCPMC2118261

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.