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Inhibition of placental trophoblast fusion by guanylate-binding protein 5

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F25%3A00645075" target="_blank" >RIV/68378050:_____/25:00645075 - isvavai.cz</a>

  • Result on the web

    <a href="https://www.science.org/doi/epdf/10.1126/sciadv.adt5388" target="_blank" >https://www.science.org/doi/epdf/10.1126/sciadv.adt5388</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1126/sciadv.adt5388" target="_blank" >10.1126/sciadv.adt5388</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Inhibition of placental trophoblast fusion by guanylate-binding protein 5

  • Original language description

    Syncytin-1 and Syncytin-2 are envelope glycoproteins encoded by human endogenous retroviruses that have been exapted for the fusion of cytotrophoblast cells into syncytiotrophoblasts during placental development. Pregnancy complications like preeclampsia are associated with altered expression of interferon-stimulated genes, including guanylate-binding protein 5 (GBP5). Here, we show that misdirected antiviral activity of GBP5 impairs processing and activation of Syncytin-1. In contrast, the proteolytic activation of Syncytin-2 is not affected by GBP5, and its fusogenic activity is only modestly reduced. Mechanistic analyses revealed that Syncytin-1 is mainly cleaved by the GBP5 target furin, whereas Syncytin-2 is also efficiently processed by the proprotein convertase subtilisin/kexin type 7 (PCSK7) and thus resistant to GBP5-mediated restriction. Mutational analyses mapped PCSK7 processing of Syncytin-2 to a leucine residue upstream of the polybasic cleavage site. In summary, we identified an innate immune mechanism that impairs the activity of a co-opted endogenous retroviral envelope protein during pregnancy and may potentially contribute to the pathogenesis of pregnancy disorders.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    <a href="/en/project/LX22NPO5103" target="_blank" >LX22NPO5103: National Institute of Virology and Bacteriology</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2025

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Science Advances

  • ISSN

    2375-2548

  • e-ISSN

    2375-2548

  • Volume of the periodical

    11

  • Issue of the periodical within the volume

    19

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    14

  • Pages from-to

    eadt5388

  • UT code for WoS article

    001483895900010

  • EID of the result in the Scopus database

    2-s2.0-105004779558