Backbone chemical shift spectral assignments of SARS coronavirus-2 non-structural protein nsp9

F. Dudás, Erika; Puglisi, Rita; Korn, Sophie Marianne; Alfano, Caterina; Bellone, Maria Laura; Piaz, Fabrizio Dal; Kelly, Geoff; Monaca, Elisa; Schlundt, Andreas; Schwalbe, Harald; Pastore, Annalisa

As part of an International consortium aiming at the characterization by NMR of the proteins of the SARS-CoV-2 virus, we have obtained the virtually complete assignment of the backbone atoms of the non-structural protein nsp9. This small (12 kDa) protein is encoded by ORF1a, binds to RNA and seems to be essential for viral RNA synthesis. The crystal structures of the SARS-CoV-2 protein and other homologues suggest that the protein is dimeric as also confirmed by analytical ultracentrifugation and dynamic light scattering. Our data constitute the prerequisite for further NMR-based characterization, and provide the starting point for the identification of small molecule lead compounds that could interfere with RNA binding and prevent viral replication.