RNASeq profiling of COVID19‐infected patients identified an EIF2AK2 inhibitor as a potent SARS‐CoV‐2 antiviral.

The HCoV-OC43 coronavirus N protein inhibitor PJ34 (indicated with carbon atom-coloured cyan) is structurally similar to C16 and binds at the same NTD nucleotide-binding pocket, justifying the hypothetical structural model of the N protein complex with C16. We also found that C16 binds to an EIF2AK2 hub interacting protein, the SARS-CoV-2 N protein, thus could act as a dual inhibitor, conferring strong SARS-CoV-2 antiviral activity. Dear Editor, In this study, we found gene expression changes in key genes involved in activating immune pathways and genes targeted by SARS-CoV-2 to interfere with normal host cell functioning. RNASeq profiling of COVID19-infected patients identified an EIF2AK2 inhibitor as a potent SARS-CoV-2 antiviral. [Extracted from the article]