Evidence map›Paper›PMID 21990358›Full record

ArticleThe Journal of biological chemistry2011

Reversible major histocompatibility complex I-peptide multimers containing Ni(2+)-nitrilotriacetic acid peptides and histidine tags improve analysis and sorting of CD8(+) T cells.

Julien Schmidt, Philippe Guillaume, Melita Irving, Petra Baumgaertner, Daniel Speiser, Immanuel F Luescher

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.5field-weighted citation impact, top 31% 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

18 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Dual CD8 and TCR editing in regulatory T cells mediates HLA-A2-restricted tissue-specific homing.Molecular therapy : the journal of the American Society of Gene Therapy · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Cancer therapy in mice using a pure population of CD8Cancer immunology, immunotherapy : CII · 2021
    Article
  8. Review
  9. Article
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  12. Article
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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 1 country.

Julien SchmidtLudwig Center of the University of Lausanne, 1066 Epalinges, Switzerland.
Philippe GuillaumeLudwig Center of the University of Lausanne, 1066 Epalinges, Switzerland.
Melita IrvingSwiss Institute of Bioinformatics, Batiment Genopode, 1015 Lausanne Switzerland.
Petra BaumgaertnerDivision of Clinical Onco-Immunology, Ludwig Center of the University of Lausanne, 1011 Lausanne, Switzerland.
Daniel SpeiserDivision of Clinical Onco-Immunology, Ludwig Center of the University of Lausanne, 1011 Lausanne, Switzerland.
Immanuel F LuescherLudwig Center of the University of Lausanne, 1066 Epalinges, Switzerland. Electronic address: immanuel.luescher@unil.ch.
Ludwig Cancer Research · CHUniversity of Lausanne · CHSIB Swiss Institute of Bioinformatics · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

MHC-peptide multimers containing biotinylated MHC-peptide complexes bound to phycoerythrin (PE) streptavidin (SA) are widely used for analyzing and sorting antigen-specific T cells. Here we describe alternative T cell-staining reagents that are superior to conventional reagents. They are built on reversible chelate complexes of Ni(2+)-nitrilotriacetic acid (NTA) with oligohistidines. We synthesized biotinylated linear mono-, di-, and tetra-NTA compounds using conventional solid phase peptide chemistry and studied their interaction with HLA-A*0201-peptide complexes containing a His(6), His(12), or 2×His(6) tag by surface plasmon resonance on SA-coated sensor chips and equilibrium dialysis. The binding avidity increased in the order His(6) < His(12) < 2×His(6) and NTA(1) < NTA(2) < NTA(4), respectively, depending on the configuration of the NTA moieties and increased to picomolar K(D) for the combination of a 2×His(6) tag and a 2×Ni(2+)-NTA(2). We demonstrate that HLA-A2-2×His(6)-peptide multimers containing either Ni(2+)-NTA(4)-biotin and PE-SA- or PE-NTA(4)-stained influenza and Melan A-specific CD8+ T cells equal or better than conventional multimers. Although these complexes were highly stable, they very rapidly dissociated in the presence of imidazole, which allowed sorting of bona fide antigen-specific CD8+ T cells without inducing T cell death as well as assessment of HLA-A2-peptide monomer dissociation kinetics on CD8+ T cells.

Indexed as

HistidineHLA-A2 AntigenPeptidesCD8-Positive T-LymphocytesHumansMART-1 AntigenNickelNitrilotriacetic AcidStaining and LabelingHistidineHLA-A*02:01 antigenHLA-A2 AntigenMART-1 AntigenMLANA protein, humanNickelNitrilotriacetic AcidPeptidespolyhistidine

Identifiers

PMID21990358
PMCPMC3308881
OpenAlexW1975042913

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.