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@ARTICLE{Srinivasan:480474,
author = {Srinivasan, Vasundara and Brognaro, Hévila and Prabhu,
Prince R. and de Souza, Edmarcia Elisa and Günther,
Sebastian and Reinke, Patrick Y. A. and Lane, Thomas J. and
Ginn, Helen and Han, Huijong and Ewert, Wiebke and Sprenger,
Janina and Koua, Faisal H. M. and Falke, Sven and Werner,
Nadine and Andaleeb, Hina and Ullah, Najeeb and Franca,
Bruno Alves and Wang, Mengying and Barra, Angélica Luana C
and Perbandt, Markus and Schwinzer, Martin and Schmidt,
Christina and Brings, Lea and Lorenzen, Kristina and
Schubert, Robin and Guaragna Machado, Rafael Rahal and
Candido, Erika Donizette and Leal Oliveira, Danielle Bruna
and Durigon, Edison Luiz and Yefanov, Oleksandr and Lieske,
Julia and Gelisio, Luca and Domaracky, Martin and
Middendorf, Philipp and Groessler, Michael and Trost, Fabian
and Galchenkova, Marina and Saouane, Sofiane and Hakanpää,
Johanna and Wolf, Markus and Turk, Dusan and Pearson, Arwen
R. and Chapman, Henry N. and Hinrichs, Winfried and Wrenger,
Carsten and Meents, Alke and Betzel, Christian},
title = {{SARS}-{C}o{V}-2 papain-like protease {PL}pro in complex
with natural compounds reveal allosteric sites for antiviral
drug design},
reportid = {PUBDB-2022-03779},
year = {2021},
abstract = {SARS-CoV-2 papain-like protease (PLpro) covers multiple
functions. Beside the cysteine-protease activity, PLpro has
the additional and vital function of removing ubiquitin and
ISG15 (Interferon-stimulated gene 15) from host-cell
proteins to aid coronaviruses in evading the host’s innate
immune responses. We established a high-throughput X-ray
screening to identify inhibitors by elucidating the native
PLpro structure refined to 1.42 Å and performing
co-crystallization utilizing a diverse library of selected
natural compounds. We identified three phenolic compounds as
potential inhibitors. Crystal structures of PLpro inhibitor
complexes, obtained to resolutions between 1.7-1.9 Å, show
that all three compounds bind at the ISG15/Ub-S2 allosteric
binding site, preventing the essential ISG15-PLpro molecular
interactions. All compounds demonstrate clear inhibition in
a deISGylation assay, two exhibit distinct antiviral
activity and one inhibited a cytopathic effect in a
non-cytotoxic concentration range. These results highlight
the druggability of the rarely explored ISG15/Ub-S2 PLpro
allosteric binding site to identify new and effective
antiviral compounds. Importantly, in the context of
increasing PLpro mutations in the evolving new variants of
SARS-CoV-2, the natural compounds we identified may also
reinstate the antiviral immune response processes of the
host that are down-regulated in COVID-19 infections.},
cin = {FS-CFEL-1-BMX / DOOR ; HAS-User / EMBL / FS-CFEL-1-PBIO /
CFEL-I / FS-PET-D / CFEL-TRSB},
cid = {I:(DE-H253)FS-CFEL-1-BMX-20210408 /
I:(DE-H253)HAS-User-20120731 / I:(DE-H253)EMBL-20120731 /
I:(DE-H253)FS-CFEL-1-PBIO-20210408 /
I:(DE-H253)CFEL-I-20161114 / I:(DE-H253)FS-PET-D-20190712 /
I:(DE-H253)CFEL-TRSB-20161025},
pnm = {633 - Life Sciences – Building Blocks of Life: Structure
and Function (POF4-633) / 6G3 - PETRA III (DESY) (POF4-6G3)},
pid = {G:(DE-HGF)POF4-633 / G:(DE-HGF)POF4-6G3},
experiment = {EXP:(DE-H253)P-P11-20150101},
typ = {PUB:(DE-HGF)25},
doi = {10.1101/2021.11.17.468943},
url = {https://bib-pubdb1.desy.de/record/480474},
}