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Audio Interview

Identifying SARS-CoV-2 proteases

Published on April 22, 2021   10 min

A selection of talks on Biochemistry

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Interviewer: Professor Muller, and Professor Gutschow, thank you very much to you both for taking the time to do this interview today with us on the research being done by you both and your team in identifying the SARS-CoV-2 proteases and designing their inhibitors. Professor Gutschow, could you please start by outlining the biology of these proteases and why inhibiting these proteases is an important factor in the treatment of COVID-19? Prof. Gutschow: Yes, two promising targets for the development of COVID-19 therapeutics emerged. These are the essential main protease and papain-like protease. The biology of these proteases and their essential role is publication are well-established. Also based on the knowledge of previous viral infections such as SARS-CoV-1 outbreak in 2003. These two cysteine proteases are encoded in the viral genome. The resulting enzymes are responsible for crucial cleavages of the viral polyprotein. The main protease liberates itself from a large body proteins, so the outer cleavage and then the major dimeric enzyme can be formed. The catalytic activity of the main protease is critical for the assembly of the viral replication transcription complex, for the release of functional viral proteins, and thus, for the replication of SARS-CoV-2. In general protease catalyze the hydrolytic cleavage of peptide bonds. Cysteine proteases constitute one group of proteases and follow an acyl transfer mechanism, which I would like to explain shortly. The active site cysteine residue attacks