Publications by authors named "Michael GroeSSler"
SARS-CoV-2 papain-like protease (PLpro) covers multiple functions. Beside the cysteine-protease activity, facilitating cleavage of the viral polypeptide chain, PLpro has the additional and vital function of removing ubiquitin and ISG15 (Interferon-stimulated gene 15) from host-cell proteins to support coronaviruses in evading the host's innate immune responses. We identified three phenolic compounds bound to PLpro, preventing essential molecular interactions to ISG15 by screening a natural compound library.
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- COVID-19, caused by SARS-CoV-2, is a severe global health crisis with no direct treatment available.
- Researchers conducted a high-throughput x-ray crystallography screen on repurposed drug libraries targeting the virus's main protease, which is crucial for its replication.
- They identified 37 compounds that bind to the protease and found two promising allosteric binding sites, with several compounds showing antiviral activity without toxicity in further tests.