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| Home > Publications database > SARS-CoV-2 papain-like protease PLpro in complex with natural compounds reveal allosteric sites for antiviral drug design > print |
| 001 | 480474 | ||
| 005 | 20221019122656.0 | ||
| 024 | 7 | _ | |a 10.1101/2021.11.17.468943 |2 doi |
| 024 | 7 | _ | |a altmetric:117376382 |2 altmetric |
| 037 | _ | _ | |a PUBDB-2022-03779 |
| 041 | _ | _ | |a English |
| 100 | 1 | _ | |a Srinivasan, Vasundara |0 P:(DE-H253)PIP1080622 |b 0 |e Corresponding author |
| 245 | _ | _ | |a SARS-CoV-2 papain-like protease PLpro in complex with natural compounds reveal allosteric sites for antiviral drug design |
| 260 | _ | _ | |c 2021 |
| 336 | 7 | _ | |a Preprint |b preprint |m preprint |0 PUB:(DE-HGF)25 |s 1666175160_16133 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a WORKING_PAPER |2 ORCID |
| 336 | 7 | _ | |a Electronic Article |0 28 |2 EndNote |
| 336 | 7 | _ | |a preprint |2 DRIVER |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a Output Types/Working Paper |2 DataCite |
| 520 | _ | _ | |a 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. |
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