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

Biomol NMR Assign. 2021 Oct;15(2):235-241. doi: 10.1007/s12104-021-10011-0. Epub 2021 Mar 23.

Abstract

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.

Keywords: Coronavirus; Covid-19 NMR; Protein; SARS-CoV-2; Solution NMR; Structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Hydrogen-Ion Concentration
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular*
  • Protein Structure, Secondary
  • RNA-Binding Proteins / chemistry*
  • Viral Nonstructural Proteins / chemistry*

Substances

  • NSP9 protein, SARS-CoV-2
  • RNA-Binding Proteins
  • Viral Nonstructural Proteins