De novo developed protein binders mimicking Interferon lambda signaling

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F21%3A00550560" target="_blank" >RIV/86652036:_____/21:00550560 - isvavai.cz</a>

Výsledek na webu

<a href="https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.16300" target="_blank" >https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.16300</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1111/febs.16300" target="_blank" >10.1111/febs.16300</a>

Jazyk výsledku

angličtina

Název v původním jazyce

De novo developed protein binders mimicking Interferon lambda signaling

Popis výsledku v původním jazyce

We hereby describe the process of design and selection of nonantibody protein binders mimicking cytokine signaling. We chose to mimic signaling of IFN-lambda 1, type 3 interferon (also known as IL-29) for its novelty and the importance of its biological functions. All four known interferons lambda signal through binding to the extracellular domains of IL-28 receptor 1 (IL-28R1) and IL-10 receptor 2 (IL-10R2). Our binders were therefore trained to bind both receptors simultaneously. The bifunctional binder molecules were developed by yeast display, a method of directed evolution. The signaling capacity of the bivalent binders was tested by measuring phosphorylation of the JAK/STAT signaling pathway and production of mRNA of six selected genes naturally induced by IFN- lambda 1 in human cell lines. The newly developed bivalent binders offer opportunities to study cytokine-related biological functions and modulation of the cell behavior by receptor activation on the cell surfaces alternative to the use of natural IFN-lambda.

Název v anglickém jazyce

De novo developed protein binders mimicking Interferon lambda signaling

Popis výsledku anglicky

We hereby describe the process of design and selection of nonantibody protein binders mimicking cytokine signaling. We chose to mimic signaling of IFN-lambda 1, type 3 interferon (also known as IL-29) for its novelty and the importance of its biological functions. All four known interferons lambda signal through binding to the extracellular domains of IL-28 receptor 1 (IL-28R1) and IL-10 receptor 2 (IL-10R2). Our binders were therefore trained to bind both receptors simultaneously. The bifunctional binder molecules were developed by yeast display, a method of directed evolution. The signaling capacity of the bivalent binders was tested by measuring phosphorylation of the JAK/STAT signaling pathway and production of mRNA of six selected genes naturally induced by IFN- lambda 1 in human cell lines. The newly developed bivalent binders offer opportunities to study cytokine-related biological functions and modulation of the cell behavior by receptor activation on the cell surfaces alternative to the use of natural IFN-lambda.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2021

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

FEBS Journal

ISSN

1742-464X

e-ISSN

1742-4658

Svazek periodika

DEC 2021

Číslo periodika v rámci svazku

2021-12-11

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

13

Strana od-do

—

Kód UT WoS článku

000727611300001

EID výsledku v databázi Scopus

2-s2.0-85120717487