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Statements

Subject Item
n2:RIV%2F00216208%3A11130%2F14%3A10293045%21RIV15-MSM-11130___
rdf:type
n16:Vysledek skos:Concept
rdfs:seeAlso
http://dx.doi.org/10.1002/prot.24472
dcterms:description
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. Proteins 2014; 82:975-989. (c) 2013 The Authors. Proteins: Structure, Function, and Bioinformatics Published by Wiley Periodicals, Inc. 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. Proteins 2014; 82:975-989. (c) 2013 The Authors. Proteins: Structure, Function, and Bioinformatics Published by Wiley Periodicals, Inc.
dcterms:title
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 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
skos:prefLabel
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 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
skos:notation
RIV/00216208:11130/14:10293045!RIV15-MSM-11130___
n3:aktivita
n5:Z n5:P n5:I
n3:aktivity
I, P(ED1.1.00/02.0109), P(GAP302/11/0580), P(GAP303/10/1849), Z(AV0Z50520701)
n3:cisloPeriodika
6
n3:dodaniDat
n9:2015
n3:domaciTvurceVysledku
n8:7400705 n8:8646597
n3:druhVysledku
n21:J
n3:duvernostUdaju
n4:S
n3:entitaPredkladatele
n20:predkladatel
n3:idSjednocenehoVysledku
19961
n3:idVysledku
RIV/00216208:11130/14:10293045
n3:jazykVysledku
n18:eng
n3:klicovaSlova
cytokine; protein scaffold; engineered binding protein; psoriasis; combinatorial library; ribosome display
n3:klicoveSlovo
n14:ribosome%20display n14:protein%20scaffold n14:engineered%20binding%20protein n14:cytokine n14:psoriasis n14:combinatorial%20library
n3:kodStatuVydavatele
US - Spojené státy americké
n3:kontrolniKodProRIV
[71F3DF99B010]
n3:nazevZdroje
Proteins: Structure, Function and Genetics
n3:obor
n19:FD
n3:pocetDomacichTvurcuVysledku
2
n3:pocetTvurcuVysledku
12
n3:projekt
n13:ED1.1.00%2F02.0109 n13:GAP303%2F10%2F1849 n13:GAP302%2F11%2F0580
n3:rokUplatneniVysledku
n9:2014
n3:svazekPeriodika
82
n3:tvurceVysledku
Sipova, Hana Maly, Petr Kalina, Tomáš Vankova, Lucie Kuchar, Milan Homola, Jiří Pelák, Ondřej Schneider, Bohdan Černý, Jiří Osicka, Radim Petrokova, Hana Sebo, Peter
n3:wos
000335955300009
n3:zamer
n12:AV0Z50520701
s:issn
0887-3585
s:numberOfPages
15
n7:doi
10.1002/prot.24472
n10:organizacniJednotka
11130