Evidence map›Paper›PMID 28352266›Full record

ArticleFrontiers in immunology2017

Canonical and Cross-reactive Binding of NK Cell Inhibitory Receptors to HLA-C Allotypes Is Dictated by Peptides Bound to HLA-C.

Malcolm J W Sim, Stacy A Malaker, Ayesha Khan, Janet M Stowell, Jeffrey Shabanowitz, Mary E Peterson, Sumati Rajagopalan, Donald F Hunt, Daniel M Altmann, Eric O Long and 1 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Frontiers in immunology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

29 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
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  7. DonorFrontiers in immunology · 2024
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  15. High-affinity oligoclonal TCRs define effective adoptive T cell therapy targeting mutant KRAS-G12D.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. Review
  17. Human NK cell receptor KIR2DS4 detects a conserved bacterial epitope presented by HLA-C.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  18. Article
  19. Review
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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

11 authors at 3 institutions in 2 countries.

Malcolm J W SimLaboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, NIH, Rockville, MD, USA; Lung Immunology Group, Department of Medicine, Imperial College London, London, UK.
Stacy A MalakerDepartment of Chemistry, University of Virginia, Charlottesville, VA, USA; Department of Chemistry, Stanford University, Stanford, CA, USA.
Ayesha KhanLung Immunology Group, Department of Medicine, Imperial College London , London , UK.
Janet M StowellLung Immunology Group, Department of Medicine, Imperial College London , London , UK.
Jeffrey ShabanowitzDepartment of Chemistry, University of Virginia , Charlottesville, VA , USA.
Mary E PetersonLaboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, NIH , Rockville, MD , USA.
Sumati RajagopalanLaboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, NIH , Rockville, MD , USA.
Donald F HuntDepartment of Chemistry, University of Virginia, Charlottesville, VA, USA; Department of Pathology, University of Virginia, Charlottesville, VA, USA.
Daniel M AltmannLung Immunology Group, Department of Medicine, Imperial College London , London , UK.
Eric O LongLaboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, NIH , Rockville, MD , USA.
Rosemary J BoytonLung Immunology Group, Department of Medicine, Imperial College London , London , UK.
Imperial College London · GBNational Institute of Allergy and Infectious Diseases · USUniversity of Virginia · US

Funding

Regulation of immune responses by inhibitory receptorsZIAAI001117 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI LONG, ERIC O · 2009 to 2019
$5.7M
PROCESSED ANTIGEN CHARACTERIZATION BY MASS SPECTROMETRYR37AI033993 · NIAID · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI HUNT, DONALD F · 1999 to 2008
$5.6M
PROCESSED ANTIGEN CHARACTERIZATION BY MASS SPECTROMETRYR01AI033993 · NIAID · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI HUNT, DONALD F · 1994 to 2017
$4.9M
NIAID NIH HHS HHSN272200900046CNIAID NIH HHS R01 AI033993NIAID NIH HHS R37 AI033993Wellcome Trust
6 · The paper itself

Abstract

backgroundHuman natural killer (NK) cell activity is regulated by a family of killer cell immunoglobulin-like receptors (KIRs) that bind human leukocyte antigen (HLA) class I. Combinations of KIR and HLA genotypes are associated with disease, including susceptibility to viral infection and disorders of pregnancy. KIR2DL1 binds HLA-C alleles of group C2 (Lys

resultsThe impact of HLA-C bound peptide on inhibitory KIR binding was investigated taking advantage of the fact that HLA-C*05:01 (HLA-C group 2, C2) and HLA-C*08:02 (HLA-C group 1, C1) have identical sequences apart from the key KIR specificity determining epitope at residues 77 and 80. Endogenous peptides were eluted from HLA-C*05:01 and used to test the peptide dependence of KIR2DL1 and KIR2DL2/3 binding to HLA-C*05:01 and HLA-C*08:02 and subsequent impact on NK cell function. Specific binding of KIR2DL1 to the C2 allotype occurred with the majority of peptides tested. In contrast, KIR2DL2/3 binding to the C1 allotype occurred with only a subset of peptides. Cross-reactive binding of KIR2DL2/3 with the C2 allotype was restricted to even fewer peptides. Unexpectedly, two peptides promoted binding of the C2 allotype-specific KIR2DL1 to the C1 allotype. We showed that presentation of endogenous peptides or HIV Gag peptides by HLA-C can promote KIR cross-reactive binding.

conclusionKIR2DL2/3 binding to C1 is more peptide selective than that of KIR2DL1 binding to C2, providing an explanation for KIR2DL3-C1 interactions appearing weaker than KIR2DL1-C2. In addition, cross-reactive binding of KIR is characterized by even higher peptide selectivity. We demonstrate a hierarchy of functional peptide selectivity of KIR-HLA-C interactions with relevance to NK cell biology and human disease associations. This selective peptide sequence-driven binding of KIR provides a potential mechanism for pathogen as well as self-peptide to modulate NK cell activation through altering levels of inhibition.

Indexed as

human leukocyte antigenimmunogeneticsinnate immunitykiller cell Ig-like receptorsnatural killer cell

Identifiers

PMID28352266
PMCPMC5348643
OpenAlexW2952762050

What OpenQuestion holds

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LicenceCC BY
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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.