The economical and societal impact of COVID-19 has made the development of vaccines and drugs to combat SARS-CoV-2 infection a priority.

While the SARS-CoV-2 spike protein has been widely explored as a drug target, the SARSCoV-2 helicase (nsp13) does not have any approved medication. The helicase shares 99.8% similarity with its SARS-CoV-1 homolog and was shown to be essential for viral replication. This review summarizes and builds on existing research on inhibitors of SARS-CoV-1 and SARS-CoV-2 helicases. Our analysis on the toxicity and specificity of these compounds, set the road going forward for the repurposing of existing drugs and the development of new SARS-CoV-2 helicase inhibitors.

Front. Chem., 2022, 10

Binding sites of SARS-CoV-Nsp13 helicase. Panel (A) Structure of SARS-CoV-Nsp13 helicase (PDB ID: 7NN0) (Newman et al., 2021). V570, the single different residue from SARS Helicase (I570) is highlighted in red. The residues constituting the ATP binding site are shown in the enlarged window bound with AMP-PNP, an AMP analog. Panel (B) Possible binding pockets from Nsp13 fragment screening. Reproduced from Newman et al., 2021 under a Creative Commons Attribution 4.0 International License

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