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Characterization and Noncovalent Inhibition of the Deubiquitinase and deISGylase Activity of SARS-CoV-2 Papain-Like Protease
Open accessAbstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent for COVID-19, is a novel human betacoronavirus that is rapidly spreading worldwide. The outbreak currently includes over 3.7 million cases and 260,000 fatalities. As a betacoronavirus, SARS-CoV-2 encodes for a papain-like protease (PLpro) that is likely responsible for cleavage of the coronavirus (CoV) viral polypeptide. The PLpro is also responsible for suppression of host innate immune responses by virtue of its ability to reverse host ubiquitination and ISGylation events. Here, the biochemical activity of SARS-CoV-2 PLpro against ubiquitin (Ub) and interferon-stimulated gene product 15 (ISG15) substrates is evaluated, revealing that the protease has a marked reduction in its ability to process K48 linked Ub substrates compared to its counterpart in SARS-CoV. Additionally, its substrate activity more closely mirrors that of the PLpro from the Middle East respiratory syndrome coronavirus and prefers ISG15s from certain species including humans. Additionally, naphthalene based PLpro inhibitors are shown to be effective at halting SARS-CoV-2 PLpro activity as well as SARS-CoV-2 replication.
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Cites
Interferon-inducible antiviral effectors
Sadler, A. J., & Williams, B. R. G. (2008) · Nature Reviews Immunology · doi:10.1038/nri2314 · Cited by 2,160
Devaraj, S. G., Wang, N., Chen, Z., Chen, Z., Tseng, M., Barretto, N., Lin, R., Peters, C. J., Tseng, C.-T. K., Baker, S. C., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704870200 · Cited by 411
Cited by
Rut, W., Lv, Z., Zmudzinski, M., Patchett, S., Nayak, D., Snipas, S. J., El Oualid, F., Huang, T. T., Bekes, M., Drag, M., et al. (2020) · Science Advances · doi:10.1126/sciadv.abd4596 · Cited by 459
Structural insights into SARS-CoV-2 proteins
Arya, R., Kumari, S., Pandey, B., Mistry, H., Bihani, S. C., Das, A., Prashar, V., Gupta, G. D., Panicker, L., & Kumar, M. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.11.024 · Cited by 348
Crystal structure of SARS-CoV-2 papain-like protease
Gao, X., Qin, B., Chen, P., Zhu, K., Hou, P., Wojdyla, J. A., Wang, M., & Cui, S. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2020.08.014 · Cited by 336
Fu, Z., Huang, B., Tang, J., Liu, S., Liu, M., Ye, Y., Liu, Z., Xiong, Y., Zhu, W., Cao, D., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-20718-8 · Cited by 322
The IUPHAR/BPS Guide to PHARMACOLOGY in 2024
Harding, S. D., Armstrong, J. F., Faccenda, E., Southan, C., Alexander, S. P. H., Davenport, A. P., Spedding, M., & Davies, J. A. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkad944 · Cited by 226
Metadata
- Authors
- Freitas, B. T., Durie, I. A., Murray, J., Longo, J. E., Miller, H. C., Crich, D., Hogan, R. J., Tripp, R. A., & Pegan, S. D.
- Venue
- ACS Infectious Diseases
- Publisher
- American Chemical Society (ACS)
- Published
- 2020-05-19
- Volume
- 6
- Issue
- 8
- Pages
- 2099-2109
- ISSN
- 2373-8227 (ISSN-L)
- OpenAlex
- W3024964904
- Cited by
- 290
- References
- 2
- FWCI
- 6.97
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Freitas, B. T., Durie, I. A., Murray, J., Longo, J. E., Miller, H. C., Crich, D., Hogan, R. J., Tripp, R. A., & Pegan, S. D. (2020). Characterization and Noncovalent Inhibition of the Deubiquitinase and deISGylase Activity of SARS-CoV-2 Papain-Like Protease. ACS Infectious Diseases. https://doi.org/10.1021/acsinfecdis.0c00168
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