Evidence map›Paper›PMID 22006319›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Structural reorganization of the antigen-binding groove of human CD1b for presentation of mycobacterial sulfoglycolipids.

Luis F Garcia-Alles, Anthony Collmann, Cees Versluis, Buko Lindner, Julie Guiard, Laurent Maveyraud, Emilie Huc, Jin S Im, Sebastiano Sansano, Thérèse Brando and 10 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

32 citing papers in PubMed, 50 citations in OpenAlex.

  1. Insights into the CD1 lipidome.Frontiers in immunology · 2024
    Article
  2. Article
  3. Article
  4. Remembering Enzo Cerundolo.Molecular immunology · 2021
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. A TCR β-Chain Motif Biases toward Recognition of Human CD1 Proteins.Journal of immunology (Baltimore, Md. : 1950) · 2019
    Article
  11. Review
  12. Molecular recognition of microbial lipid-based antigens by T cells.Cellular and molecular life sciences : CMLS · 2018
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Four pathways of CD1 antigen presentation to T cells.Current opinion in immunology · 2017
    Review
  18. Review
  19. Review
  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

20 authors at 11 institutions in 6 countries.

Luis F Garcia-AllesCentre National de la Recherche Scientifique, Institut de Pharmacologie et de Biologie Structurale, F-31077 Toulouse, France.
Anthony Collmann
Cees Versluis
Buko Lindner
Julie Guiard
Laurent Maveyraud
Emilie Huc
Jin S Im
Sebastiano Sansano
Thérèse Brando
Sylviane Julien
Jacques Prandi
Martine Gilleron
Steven A Porcelli
Henri de la Salle
Albert J R Heck
Lucia Mori
Germain Puzo
Lionel Mourey
Gennaro De Libero
Université Toulouse III - Paul Sabatier · FRUniversité Fédérale de Toulouse Midi-Pyrénées · FRInstitut de Pharmacologie et de Biologie Structurale · FRUniversity Hospital of Basel · CHUtrecht University · NLAgency for Science, Technology and Research · SGAlbert Einstein College of Medicine · USÉtablissement Français du Sang · FRResearch Center Borstel - Leibniz Lung Center · DEUniversity of Basel · CHYeshiva University · US

Funding

Precision Targeting of CD1-Restricted iNKT Cells for Cancer ImmunotherapyR01AI045889 · NIAID · YESHIVA UNIVERSITY · PI Steven A Porcelli · 1999 to 2026
$9.3M
NIAID NIH HHS AI45889NIAID NIH HHS R01 AI045889
6 · The paper itself

Abstract

The mechanisms permitting nonpolymorphic CD1 molecules to present lipid antigens that differ considerably in polar head and aliphatic tails remain elusive. It is also unclear why hydrophobic motifs in the aliphatic tails of some antigens, which presumably embed inside CD1 pockets, contribute to determinants for T-cell recognition. The 1.9-Å crystal structure of an active complex of CD1b and a mycobacterial diacylsulfoglycolipid presented here provides some clues. Upon antigen binding, endogenous spacers of CD1b, which consist of a mixture of diradylglycerols, moved considerably within the lipid-binding groove. Spacer displacement was accompanied by F' pocket closure and an extensive rearrangement of residues exposed to T-cell receptors. Such structural reorganization resulted in reduction of the A' pocket capacity and led to incomplete embedding of the methyl-ramified portion of the phthioceranoyl chain of the antigen, explaining why such hydrophobic motifs are critical for T-cell receptor recognition. Mutagenesis experiments supported the functional importance of the observed structural alterations for T-cell stimulation. Overall, our data delineate a complex molecular mechanism combining spacer repositioning and ligand-induced conformational changes that, together with pocket intricacy, endows CD1b with the required molecular plasticity to present a broad range of structurally diverse antigens.

Indexed as

Models, MolecularProtein ConformationAntigens, CD1Chromatography, Thin LayerCrystallography, X-RayFourier AnalysisGlycolipidsHumansMutagenesisMycobacterium tuberculosisSpectrometry, Mass, Electrospray IonizationAntigens, CD1CD1b antigenGlycolipidssulfoglycolipids

Identifiers

PMID22006319
PMCPMC3203780
OpenAlexW2083747911

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.