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H, 13C, and 15N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e Sophie M. Korn1,4   · Karthikeyan Dhamotharan1,4   · Boris Fürtig2,4   · Martin Hengesbach2,4   · Frank Löhr3,4   · Nusrat S. Qureshi2,4 · Christian Richter2,4 · Krishna Saxena2,4 · Harald Schwalbe2,4   · Jan‑Niklas Tants1,4   · Julia E. Weigand5   · Jens Wöhnert1,4   · Andreas Schlundt1,4  Received: 22 June 2020 / Accepted: 31 July 2020 © The Author(s) 2020

Abstract The ongoing pandemic caused by the Betacoronavirus SARS-CoV-2 (Severe Acute Respiratory Syndrome Coronavirus-2) demonstrates the urgent need of coordinated and rapid research towards inhibitors of the COVID-19 lung disease. The covid19-nmr consortium seeks to support drug development by providing publicly accessible NMR data on the viral RNA elements and proteins. The SARS-CoV-2 genome encodes for approximately 30 proteins, among them are the 16 so-called non-structural proteins (Nsps) of the replication/transcription complex. The 217-kDa large Nsp3 spans one polypeptide chain, but comprises multiple independent, yet functionally related domains including the viral papain-like protease. The Nsp3e sub-moiety contains a putative nucleic acid-binding domain (NAB) with so far unknown function and consensus target sequences, which are conceived to be both viral and host RNAs and DNAs, as well as protein-protein interactions. Its NMR-suitable size renders it an attractive object to study, both for understanding the SARS-CoV-2 architecture and drugability besides the classical virus’ proteases. We here report the near-complete NMR backbone chemical shifts of the putative Nsp3e NAB that reveal the secondary structure and compactness of the domain, and provide a basis for NMR-based investigations towards understanding and interfering with RNA- and small-molecule-binding by Nsp3e. Keywords  SARS-CoV-2 · Non-structural protein · Nucleic acid-binding domain · Solution NMR-spectroscopy · Protein drugability · Covid19-NMR

Biological context * Andreas Schlundt [email protected]‑frankfurt.de; covid19‑[email protected]‑frankfurt.de 1



Institute for Molecular Biosciences, Johann Wolfgang Goethe-University Frankfurt, Max‑von‑Laue‑Str. 9, 60438 Frankfurt, Germany

2



Institute for Organic Chemistry and Chemical Biology, Johann Wolfgang Goethe-University Frankfurt, Max‑von‑Laue‑Str. 7, 60438 Frankfurt, Germany

3

Institute of Biophysical Chemistry, Johann Wolfgang Goethe-University Frankfurt, Max‑von‑Laue‑Str. 9, 60438 Frankfurt, Germany

4

Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-University Frankfurt, 60438 Frankfurt, Germany

5

Department of Biology, Technical University of Darmstadt, Schnittspahnstr. 10, 64287 Darmstadt, Germany







SARS-CoV-2, the cause of the early 2020 pandemic accompanied by the respiratory disease called COVID-19, is the latest representative of the coronaviridae family, which also comprises the 2002 first generation SARS-CoV and the Middle East Respiratory Syn

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