% IMPORTANT: The following is UTF-8 encoded. This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.
@ARTICLE{Chatziefthymiou:631520,
author = {Chatziefthymiou, Spyros D. and Kuzikov, Maria and Afandi,
Sara and Kovacs, Greta and Srivastava, Sukrit and Zaliani,
Andrea and Gruzinov, Andrey and Pompidor, Guillaume and
Lunelli, Michele and Ahmed, Golam Rizvee and Labahn, Jörg
and Hakanpää, Johanna and Windshügel, Björn and Kolbe,
Michael},
title = {{I}dentification, validation, and characterization of
approved and investigational drugs interfering with the
{SARS} ‐ {C}o{V} ‐2 endoribonuclease {N}sp15},
journal = {Protein science},
volume = {34},
number = {6},
issn = {0961-8368},
address = {Hoboken, NJ},
publisher = {Wiley},
reportid = {PUBDB-2025-02032},
pages = {e70156},
year = {2025},
note = {This research was funded by the DESY Strategic Fund (DSF)
and by the Horizon Europe Framework Programme (grant
agreement number 101137192, AVI-THRAPID).},
abstract = {Since the emergence of SARS-CoV-2 at the end of 2019, the
virus has caused significant global health and economic
disruptions. Despite the rapid development of antiviral
vaccines and some approved treatments such as remdesivir and
paxlovid, effective antiviral pharmacological treatments for
COVID-19 patients remain limited. This study explores Nsp15,
a 3′-uridylate-specific RNA endonuclease, which has a
critical role in immune system evasion and hence in escaping
the innate immune sensors. We conducted a comprehensive drug
repurposing screen and identified 44 compounds that showed
more than $55\%$ inhibition of Nsp15 activity in a real-time
fluorescence assay. A validation pipeline was employed to
exclude unspecific interactions, and dose–response assays
confirmed 29 compounds with an IC$_{50}$ below 10 μM.
Structural studies, including molecular docking and x-ray
crystallography, revealed key interactions of identified
inhibitors, such as TAS-103 and YM-155, with the Nsp15
active site and other critical regions. Our findings show
that the identified compounds, particularly those retaining
potency under different assay conditions, could serve as
promising hits for developing Nsp15 inhibitors.
Additionally, the study emphasizes the potential of
combination therapies targeting multiple viral processes to
enhance treatment efficacy and reduce the risk of drug
resistance. This research contributes to the ongoing efforts
to develop effective antiviral therapies for SARS-CoV-2 and
possibly other coronaviruses.},
cin = {CSSB-HZI-MK / CSSB-CF-SPC},
ddc = {610},
cid = {I:(DE-H253)CSSB-HZI-MK-20210520 /
I:(DE-H253)CSSB-CF-SPC-20210520},
pnm = {633 - Life Sciences – Building Blocks of Life: Structure
and Function (POF4-633)},
pid = {G:(DE-HGF)POF4-633},
experiment = {EXP:(DE-H253)P-P11-20150101 / EXP:(DE-H253)P-P12-20150101},
typ = {PUB:(DE-HGF)16},
doi = {10.1002/pro.70156},
url = {https://bib-pubdb1.desy.de/record/631520},
}