ArticleScientific reports2016
X-Ray Structure and Inhibition of 3C-like Protease from Porcine Epidemic Diarrhea Virus.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Chebulinic acid suppresses porcine epidemic diarrhea virus infection by inhibiting viral entry and viral main protease.Frontiers in cellular and infection microbiology · 2025Article
- Assessment of optimized FRET substrates as universal corona- and picornavirus main protease substrates for screening assays.RSC advances · 2024Article
- Identification of Potent, Broad-Spectrum Coronavirus Main Protease Inhibitors for Pandemic Preparedness.Journal of medicinal chemistry · 2024Article
- Potent Antiviral Activity of Vitamin B12 against Severe Acute Respiratory Syndrome Coronavirus 2, Middle East Respiratory Syndrome Coronavirus, and Human Coronavirus 229E.Microorganisms · 2023Article
- Failure to experimentally infect 10 days-old piglets with a cell culture-propagated infectious stock of a classical genotype 1a porcine epidemic diarrhea virus.Frontiers in veterinary science · 2023Article
- Review
- Preclinical characterization of an intravenous coronavirus 3CL protease inhibitor for the potential treatment of COVID19.Nature communications · 2021Article
- Crystal Structure of SARS-CoV-2 Main Protease in Complex with the Non-Covalent Inhibitor ML188.Viruses · 2021Article
- In silico analysis of echinocandins binding to the main proteases of coronaviruses PEDV (3CLIn silico pharmacology · 2021Article
- Review
- Porcine Epidemic Diarrhea Virus and the Host Innate Immune Response.Pathogens (Basel, Switzerland) · 2020Review
- Identification of two antiviral inhibitors targeting 3C-like serine/3C-like protease of porcine reproductive and respiratory syndrome virus and porcine epidemic diarrhea virus.Veterinary microbiology · 2018Article
- Porcine Epidemic Diarrhea Virus 3C-Like Protease-Mediated Nucleocapsid Processing: Possible Link to Viral Cell Culture Adaptability.Journal of virology · 2017Article
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Authors and funding
3 authors.
Funding
Abstract
Porcine epidemic diarrhea virus (PEDV) is a coronavirus that infects pigs and can have mortality rates approaching 100% in piglets, causing serious economic impact. The 3C-like protease (3CL(pro)) is essential for the coronaviral life cycle and is an appealing target for the development of therapeutics. We report the expression, purification, crystallization and 2.10 Å X-ray structure of 3CL(pro) from PEDV. Analysis of the PEDV 3CL(pro) structure and comparison to other coronaviral 3CL(pro)'s from the same alpha-coronavirus phylogeny shows that the overall structures and active site architectures across 3CL(pro)'s are conserved, with the exception of a loop that comprises the protease S2 pocket. We found a known inhibitor of severe acute respiratory syndrome coronavirus (SARS-CoV) 3CL(pro), (R)-16, to have inhibitor activity against PEDV 3CL(pro), despite that SARS-3CL(pro) and PEDV 3CL(pro) share only 45.4% sequence identity. Structural comparison reveals that the majority of residues involved in (R)-16 binding to SARS-3CL(pro) are conserved in PEDV-3CL(pro); however, the sequence variation and positional difference in the loop forming the S2 pocket may account for large observed difference in IC50 values. This work advances our understanding of the subtle, but important, differences in coronaviral 3CL(pro) architecture and contributes to the broader structural knowledge of coronaviral 3CL(pro)'s.
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