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

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

Original languageEnglish
Pages (from-to)235-241
Number of pages7
JournalBiomolecular NMR Assignments
Issue number2
PublishedOct 2021

Bibliographical note

Funding Information: Work at BMRZ was supported by the state of Hesse. Work on Covid19-nmr was supported by the Goethe Corona Funds, by the IWB-EFRE-programme 20007375 of state of Hesse, and the DFG through CRC902: “Molecular Principles of RNA-based regulation” and through infrastructure funds (project numbers: 277478796, 277479031, 392682309, 452632086, 70653611). CA was supported by Patto per il Sud Regione Siciliana–Grant “CheMISt” (CUP G77B17000110001), and PO FESR Sicilia 2014/2020 Azione 1.5.1.—Grant “Potenziamento Infrastruttura di Ricerca “GMP Facility, Laboratori di Ricerca e Servizi Diagnostici e Terapeutici IRCCS-ISMETT” (CUP G76G17000130007), Partnership IRCCS-ISMETT/Fondazione Ri.MED. CA also acknowledges the ATeN Center of University of Palermo for infrastructures support. AP was supported by the Francis Crick Institute through provision of access to the MRC Biomedical NMR Centre. The Francis Crick Institute receives its core funding from Cancer Research UK (FC001029), the UK Medical Research Council (FC001029), and the Wellcome Trust (FC001029). Publisher Copyright: © 2021, The Author(s). Copyright: Copyright 2021 Elsevier B.V., All rights reserved.

King's Authors


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.

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