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@ARTICLE{Krchlikova:278563,
author = {Krchlikova, Veronika and Braun, Elisabeth and Weiss,
Johanna and Stafl, Krystof and Jech, Lukas and
Badarinarayan, Smitha Srinivasachar and Lotke, Rishikesh and
Travnicek, Martin and Baur, Charlotte and Stark, Paul and
Haussmann, Isabell and Lu, Yueshuang and Petersen, Moritz
and Cui, Wen and Wang, Wei and Fäger, Bianca M and
Reisinger, Hannah and Tokunaga, Kenzo and Cingöz, Oya and
Sparrer, Konstantin M J and Salker, Madhuri S and Hejnar,
Jiri and Kirchhoff, Frank and Trejbalova, Katerina and
Sauter, Daniel},
title = {{I}nhibition of placental trophoblast fusion by
guanylate-binding protein 5.},
journal = {Science advances},
volume = {11},
number = {19},
issn = {2375-2548},
address = {Washington, DC [u.a.]},
publisher = {Assoc.},
reportid = {DZNE-2025-00596},
pages = {eadt5388},
year = {2025},
abstract = {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.},
keywords = {Humans / Trophoblasts: metabolism / Trophoblasts: cytology
/ Female / Pregnancy / Pregnancy Proteins: metabolism /
Pregnancy Proteins: genetics / GTP-Binding Proteins:
metabolism / GTP-Binding Proteins: genetics / Furin:
metabolism / Placenta: metabolism / Placenta: cytology /
Gene Products, env: metabolism / Gene Products, env:
genetics / Cell Fusion / Pregnancy Proteins (NLM Chemicals)
/ GTP-Binding Proteins (NLM Chemicals) / Furin (NLM
Chemicals) / Gene Products, env (NLM Chemicals) / syncytin
(NLM Chemicals)},
cin = {AG Sparrer},
ddc = {500},
cid = {I:(DE-2719)1910003},
pnm = {351 - Brain Function (POF4-351)},
pid = {G:(DE-HGF)POF4-351},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:40333975},
pmc = {pmc:PMC12057675},
doi = {10.1126/sciadv.adt5388},
url = {https://pub.dzne.de/record/278563},
}