Evidence map›Paper›PMID 26096968›Full record

ArticleJournal of immunological methods2015

The production of KIR-Fc fusion proteins and their use in a multiplex HLA class I binding assay.

Hugo G Hilton, Achim K Moesta, Lisbeth A Guethlein, Jeroen Blokhuis, Peter Parham, Paul J Norman

Abstract read
In one paragraph

Article in Journal of immunological methods, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

17 citing papers in PubMed, 22 citations in OpenAlex.

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  8. 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
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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 2 institutions in 1 country.

Hugo G HiltonDepartment of Structural Biology, Stanford University School of Medicine, Stanford, USA; Department of Microbiology & Immunology, Stanford University School of Medicine, Stanford, USA.
Achim K MoestaDiscovery Research, Amgen Inc., South San Francisco, CA, USA.
Lisbeth A GuethleinDepartment of Structural Biology, Stanford University School of Medicine, Stanford, USA; Department of Microbiology & Immunology, Stanford University School of Medicine, Stanford, USA.
Jeroen BlokhuisDepartment of Structural Biology, Stanford University School of Medicine, Stanford, USA; Department of Microbiology & Immunology, Stanford University School of Medicine, Stanford, USA.
Peter ParhamDepartment of Structural Biology, Stanford University School of Medicine, Stanford, USA; Department of Microbiology & Immunology, Stanford University School of Medicine, Stanford, USA.
Paul J NormanDepartment of Structural Biology, Stanford University School of Medicine, Stanford, USA; Department of Microbiology & Immunology, Stanford University School of Medicine, Stanford, USA. Electronic address: paul.norman@stanford.edu.
Stanford University · USAmgen (United States) · US

Funding

MOLECULAR &CELLULAR IMMUNOBIOLOGYT32AI007290 · NIAID · STANFORD UNIVERSITY · PI Sean Curtis Bendall, Olivia M Martinez · 1985 to 2026
$27.0M
STRUCTURAL BIOLOGY OF HLA-A,B ANTIGENSR01AI017892 · NIAID · STANFORD UNIVERSITY · PI PARHAM, PETER R · 1985 to 2019
$6.1M
INTERACTIONS BETWEEN HLA CLASS I &CYTOLYTIC LYMPHOCYTESR01AI022039 · NIAID · STANFORD UNIVERSITY · PI PARHAM, PETER R · 1985 to 2017
$5.2M
NIAID NIH HHS R01 AI017892NIAID NIH HHS R01 AI022039NIAID NIH HHS T32 AI007290
6 · The paper itself

Abstract

Soluble recombinant proteins that comprise the extracellular part of a surface expressed receptor attached to the Fc region of an IgG antibody have facilitated the determination of ligand specificity for an array of immune system receptors. Among such receptors is the family of killer cell immunoglobulin-like receptors (KIR) that recognize HLA class I ligands. These receptors, expressed on natural killer (NK) cells and T cells, play important roles in both immune defense and placental development in early pregnancy. Here we describe a method for the production of two domain KIR-Fc fusion proteins using baculovirus infected insect cells. This method is more scalable than traditional mammalian cell expression systems and produces efficiently folded proteins that carry posttranslational modifications found in native KIR. We also describe a multiplex binding assay using the Luminex platform that determines the avidity and specificity of two domain KIR-Fc for a panel of microbeads, each coated with one of 97 HLA class I allotypes. This assay is simple to perform, and represents a major improvement over the assays used previously, which were limited in the number of KIR and HLA class I combinations that could be assayed at any one time. The results obtained from this assay can be used to predict the response of NK cell and T cells when their KIR recognize HLA class I.

Indexed as

AnimalsBaculoviridaeBiological AssayCell LineHistocompatibility Antigens Class IImmunoglobulin Fc FragmentsInsectaKiller Cells, NaturalLigandsProtein BindingProtein FoldingReceptors, Antigen, T-CellReceptors, KIRReceptors, Natural Killer CellRecombinant ProteinsSf9 CellsHistocompatibility Antigens Class IImmunoglobulin Fc FragmentsLigandsReceptors, Antigen, T-CellReceptors, KIRReceptors, Natural Killer CellRecombinant ProteinsAntigens/peptides/epitopesComparative immunology/evolutionMHCNatural killer cells

Identifiers

PMID26096968
PMCPMC4604020
OpenAlexW829954470

What OpenQuestion holds

Textmetadata
LicenceTDM
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.