Evidence map›Paper›PMID 24549990›Full record

ArticleProteins2014

Human interleukin-23 receptor antagonists derived from an albumin-binding domain scaffold inhibit IL-23-dependent ex vivo expansion of IL-17-producing T-cells.

Milan Kuchař, Lucie Vaňková, Hana Petroková, Jiří Cerný, Radim Osička, Ondřej Pelák, Hana Sípová, Bohdan Schneider, Jiří Homola, Peter Sebo and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Proteins, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
1.3field-weighted citation impact, top 21% 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

21 citing papers in PubMed, 1 synthesis or guideline pooled it, 37 citations in OpenAlex.

  1. Pooled it
  2. Oral delivery of recombinantDrug delivery · 2026
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  3. Review
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  15. EngineeredMicroorganisms · 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

12 authors at 4 institutions in 1 country.

Milan KuchařLaboratory of Ligand Engineering, Institute of Biotechnology AS CR, v. v. i., Vídeňská 1083, 142 20 Prague, Czech Republic.
Lucie Vaňková
Hana Petroková
Jiří Cerný
Radim Osička
Ondřej Pelák
Hana Sípová
Bohdan Schneider
Jiří Homola
Peter Sebo
Tomáš Kalina
Petr Malý
Czech Academy of Sciences, Institute of Biotechnology · CZCharles University · CZCzech Academy of Sciences, Institute of Microbiology · CZCzech Academy of Sciences, Institute of Photonics and Electronics · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Engineered combinatorial libraries derived from small protein scaffolds represent a powerful tool for generating novel binders with high affinity, required specificity and designed inhibitory function. This work was aimed to generate a collection of recombinant binders of human interleukin-23 receptor (IL-23R), which is a key element of proinflammatory IL-23-mediated signaling. A library of variants derived from the three-helix bundle scaffold of the albumin-binding domain (ABD) of streptococcal protein G and ribosome display were used to select for high-affinity binders of recombinant extracellular IL-23R. A collection of 34 IL-23R-binding proteins (called REX binders), corresponding to 18 different sequence variants, was used to identify a group of ligands that inhibited binding of the recombinant p19 subunit of IL-23, or the biologically active human IL-23 cytokine, to the recombinant IL-23R or soluble IL-23R-IgG chimera. The strongest competitors for IL-23R binding in ELISA were confirmed to recognize human IL-23R-IgG in surface plasmon resonance experiments, estimating the binding affinity in the sub- to nanomolar range. We further demonstrated that several REX variants bind to human leukemic cell lines K-562, THP-1 and Jurkat, and this binding correlated with IL-23R cell-surface expression. The REX125, REX009 and REX128 variants competed with the p19 protein for binding to THP-1 cells. Moreover, the presence of REX125, REX009 and REX115 variants significantly inhibited the IL-23-driven expansion of IL-17-producing primary human CD4(+) T-cells. Thus, we conclude that unique IL-23R antagonists derived from the ABD scaffold were generated that might be useful in designing novel anti-inflammatory biologicals.

Indexed as

Amino Acid SequenceAnti-Inflammatory AgentsBacterial ProteinsBinding, CompetitiveDrug Evaluation, PreclinicalHumansImmunologic FactorsInterleukin-23Jurkat CellsK562 CellsMolecular Sequence DataPeptide FragmentsProtein BindingReceptors, InterleukinSequence Homology, Amino AcidTh17 CellsAnti-Inflammatory AgentsBacterial ProteinsIgG Fc-binding protein, StreptococcusIL23R protein, humanImmunologic FactorsInterleukin-23Peptide FragmentsReceptors, Interleukincombinatorial librarycytokineengineered binding proteinprotein scaffoldpsoriasisribosome display

Identifiers

PMID24549990
PMCPMC4285857
OpenAlexW1534782054

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.