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Nucleocapsid protein plays crucial roles in the life cycle of SARS-CoV-2, including the formation of the ribonucleoprotein complex with viral RNA.
Structural insights into the SARS-CoV-2 nucleocapsid protein identify ceftriaxone sodium as a potential inhibitor of viral RNP complex formation, providing a basis for antiviral drug design.
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Reveals novel NTD tetramer and RNA-binding mode in SARS-CoV-2; leaves open whether these structures enable antiviral design.
Nucleocapsid (N) protein plays crucial roles in the life cycle of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), including the formation of ribonucleoprotein (RNP) complex with the viral RNA. Here we reported the crystal structures of the N-terminal domain (NTD) and C-terminal domain (CTD) of the N protein and an NTD-RNA complex. Our structures reveal a unique tetramer organization of NTD and identify a distinct RNA binding mode in the NTD-RNA complex, which could contribute to the formation of the RNP complex. We also screened small molecule inhibitors of N-NTD and N-CTD and discovered that ceftriaxone sodium, an antibiotic, can block the binding of RNA to NTD and inhibit the formation of the RNP complex. These results together could facilitate the further research of antiviral drug design targeting N protein.
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Luan et al. (2022) studied this question.
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