QUANTITATIVE ANALYSIS OF SYNCYTIN-1 BINDING TO ITS RECEPTOR

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F22%3A00567915" target="_blank" >RIV/68378050:_____/22:00567915 - isvavai.cz</a>

Výsledek na webu

<a href="http://www.ccsss.cz/index.php/ccsss/issue/view/37/67" target="_blank" >http://www.ccsss.cz/index.php/ccsss/issue/view/37/67</a>

DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

QUANTITATIVE ANALYSIS OF SYNCYTIN-1 BINDING TO ITS RECEPTOR

Popis výsledku v původním jazyce

Syncytin-1 is a fusogenic glycoprotein of retroviral origin that is specifically expressed in the human placenta. Syncytin-1 induces the fusion of cellular membranes of cytotrophoblasts after interaction with its cellular receptor, ASCT2. This process results in the formation of a multi-nuclear syncytiotrophoblast layer, which facilitates the transport of nutrients and metabolites between the mother and the fetus and is required for a successful pregnancy. Mutations in Syncytin-1 or ASCT2 can impair their interaction which may lead to disorders like eclampsia, recurrent pregnancy loss or idiopathic infertility. Up to now, aproper description of the Syncytin-1-ASCT2 binding is missing.We developed a multi-level approach to functionally analyze the efficiency of the Syncytin-1-ASCT2 interaction in a cell system. Ectopically expressed variants of ASCT2 are combined with fluorescent and luminescent proteins and can be instantly detected by microscopy, flow cytometry and common plate readers. We can routinely check for the receptor expression on mRNA and protein levels and validate its localization. We also prepared tools employing Syncytin-1: specific immunoadhesin, infectious virus and reporter cells detecting cellular fusion. With these tools, we can assess ASCT2 ability to bind and prime Syncytin-1.Our system can facilitate precise characterization of the Syncytin-1 binding site on the receptor and lead to detailed molecular understanding of one of the critical steps in human placenta morphogenesis.

Název v anglickém jazyce

QUANTITATIVE ANALYSIS OF SYNCYTIN-1 BINDING TO ITS RECEPTOR

Popis výsledku anglicky

Syncytin-1 is a fusogenic glycoprotein of retroviral origin that is specifically expressed in the human placenta. Syncytin-1 induces the fusion of cellular membranes of cytotrophoblasts after interaction with its cellular receptor, ASCT2. This process results in the formation of a multi-nuclear syncytiotrophoblast layer, which facilitates the transport of nutrients and metabolites between the mother and the fetus and is required for a successful pregnancy. Mutations in Syncytin-1 or ASCT2 can impair their interaction which may lead to disorders like eclampsia, recurrent pregnancy loss or idiopathic infertility. Up to now, aproper description of the Syncytin-1-ASCT2 binding is missing.We developed a multi-level approach to functionally analyze the efficiency of the Syncytin-1-ASCT2 interaction in a cell system. Ectopically expressed variants of ASCT2 are combined with fluorescent and luminescent proteins and can be instantly detected by microscopy, flow cytometry and common plate readers. We can routinely check for the receptor expression on mRNA and protein levels and validate its localization. We also prepared tools employing Syncytin-1: specific immunoadhesin, infectious virus and reporter cells detecting cellular fusion. With these tools, we can assess ASCT2 ability to bind and prime Syncytin-1.Our system can facilitate precise characterization of the Syncytin-1 binding site on the receptor and lead to detailed molecular understanding of one of the critical steps in human placenta morphogenesis.

Druh

O - Ostatní výsledky

CEP obor

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OECD FORD obor

10607 - Virology

Projekt

<a href="/cs/project/LX22NPO5103" target="_blank" >LX22NPO5103: Národní institut virologie a bakteriologie</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2022

Kód důvěrnosti údajů

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