Evidence map›Paper›PMID 26599805›Full record

ArticlePloS one2015

Species Specific Differences of CD1d Oligomer Loading In Vitro.

Daniel Paletta, Alina Suzann Fichtner, Lisa Starick, Steven A Porcelli, Paul B Savage, Thomas Herrmann

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 40% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Detergents alter the stability and lipid binding properties of the CD1d immunoreceptor.Protein science : a publication of the Protein Society · 2026
    Article
  2. Article
  3. 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

6 authors at 3 institutions in 2 countries.

Daniel PalettaInstitute for Virology and Immunobiology, University of Würzburg, Würzburg, Germany.
Alina Suzann FichtnerInstitute for Virology and Immunobiology, University of Würzburg, Würzburg, Germany.
Lisa StarickInstitute for Virology and Immunobiology, University of Würzburg, Würzburg, Germany.
Steven A PorcelliDepartment of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY 10461, United States of America.
Paul B SavageDepartment of Chemistry, Brigham Young University, Provo, UT 84602, United States of America.
Thomas HerrmannInstitute for Virology and Immunobiology, University of Würzburg, Würzburg, Germany.
University of Würzburg · DEAlbert Einstein College of Medicine · USBrigham Young University · US

Funding

NIAID NIH HHS HHSN272201300006C
6 · The paper itself

Abstract

CD1d molecules are MHC class I-like molecules that present glycolipids to iNKT cells. The highly conserved interaction between CD1d:α-Galactosylceramide (αGC) complexes and the iNKT TCR not only defines this population of αβ T cells but can also be used for its direct identification. Therefore, CD1d oligomers are a widely used tool for iNKT cell related investigations. To this end, the lipid chains of the antigen have to be inserted into the hydrophobic pockets of the CD1d binding cleft, often with help of surfactants. In this study, we investigated the influence of different surfactants (Triton X-100, Tween 20, Tyloxapol) on in vitro loading of CD1d molecules derived from four different species (human, mouse, rat and cotton rat) with αGC and derivatives carrying modifications of the acyl-chain (DB01-1, PBS44) and a 6-acetamido-6-deoxy-addition at the galactosyl head group (PBS57). We also compared rat CD1d dimers with tetramers and staining of an iNKT TCR transductant was used as readout for loading efficacy. The results underlined the importance of CD1d loading efficacy for proper analysis of iNKT TCR binding and demonstrated the necessity to adjust loading conditions for each oligomer/glycolipid combination. The efficient usage of surfactants as a tool for CD1d loading was revealed to be species-specific and depending on the origin of the CD1d producing cells. Additional variation of surfactant-dependent loading efficacy between tested glycolipids was influenced by the acyl-chain length and the modification of the galactosyl head group with PBS57 showing the least dependence on surfactants and the lowest degree of species-dependent differences.

Indexed as

Protein MultimerizationAmino Acid SequenceAnimalsAntigens, CD1dCell LineGlycolipidsHumansMiceMolecular Sequence DataNatural Killer T-CellsProtein BindingRatsSequence AlignmentSpecies SpecificitySurface-Active AgentsAntigens, CD1dGlycolipidsSurface-Active Agents

Identifiers

PMID26599805
PMCPMC4657966
OpenAlexW2258784854

What OpenQuestion holds

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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.