Details
| Original language | English |
|---|---|
| Pages (from-to) | 287-295 |
| Number of pages | 9 |
| Journal | Biomolecular NMR assignments |
| Volume | 15 |
| Issue number | 2 |
| Early online date | 26 Mar 2021 |
| Publication status | Published - Oct 2021 |
Abstract
The current COVID-19 pandemic caused by the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) has become a worldwide health crisis, necessitating coordinated scientific research and urgent identification of new drug targets for treatment of 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 comprises a single RNA of about 30 kb in length, in which 14 open reading frames (ORFs) have been annotated, and encodes approximately 30 proteins. The first two-thirds of the SARS-CoV-2 genome is made up of two large overlapping open-reading-frames (ORF1a and ORF1b) encoding a replicase polyprotein, which is subsequently cleaved to yield 16 so-called non-structural proteins. The non-structural protein 1 (Nsp1), which is considered to be a major virulence factor, suppresses host immune functions by associating with host ribosomal complexes at the very end of its C-terminus. Furthermore, Nsp1 facilitates initiation of viral RNA translation via an interaction of its N-terminal domain with the 5′ untranslated region (UTR) of the viral RNA. Here, we report the near-complete backbone chemical-shift assignments of full-length SARS-CoV-2 Nsp1 (19.8 kDa), which reveal the domain organization, secondary structure and backbone dynamics of Nsp1, and which will be of value to further NMR-based investigations of both the biochemical and physiological functions of Nsp1.
Keywords
- 5′ untranslated region, New drug targets, NMR spectroscopy, Non-structural proteins, Nsp1, SARS-CoV-2
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Structural Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
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In: Biomolecular NMR assignments, Vol. 15, No. 2, 10.2021, p. 287-295.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - 1H, 13C, and 15N backbone chemical-shift assignments of SARS-CoV-2 non-structural protein 1 (leader protein)
AU - Wang, Ying
AU - Kirkpatrick, John
AU - zur Lage, Susanne
AU - Korn, Sophie M.
AU - Neißner, Konstantin
AU - Schwalbe, Harald
AU - Schlundt, Andreas
AU - Carlomagno, Teresa
N1 - Funding Information: Open Access funding enabled and organized by Projekt DEAL. This work was funded by Goethe Corona Funds, the Deutsche Forschungsgemeinschaft through grant SFB902/B18 (to covid19-nmr), DFG large scale equipment grant 452632086, EU commission access programme iNEXT-discovery (grant agreement no. 871037), and grant CA294/16-1 to T.C.
PY - 2021/10
Y1 - 2021/10
N2 - The current COVID-19 pandemic caused by the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) has become a worldwide health crisis, necessitating coordinated scientific research and urgent identification of new drug targets for treatment of 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 comprises a single RNA of about 30 kb in length, in which 14 open reading frames (ORFs) have been annotated, and encodes approximately 30 proteins. The first two-thirds of the SARS-CoV-2 genome is made up of two large overlapping open-reading-frames (ORF1a and ORF1b) encoding a replicase polyprotein, which is subsequently cleaved to yield 16 so-called non-structural proteins. The non-structural protein 1 (Nsp1), which is considered to be a major virulence factor, suppresses host immune functions by associating with host ribosomal complexes at the very end of its C-terminus. Furthermore, Nsp1 facilitates initiation of viral RNA translation via an interaction of its N-terminal domain with the 5′ untranslated region (UTR) of the viral RNA. Here, we report the near-complete backbone chemical-shift assignments of full-length SARS-CoV-2 Nsp1 (19.8 kDa), which reveal the domain organization, secondary structure and backbone dynamics of Nsp1, and which will be of value to further NMR-based investigations of both the biochemical and physiological functions of Nsp1.
AB - The current COVID-19 pandemic caused by the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) has become a worldwide health crisis, necessitating coordinated scientific research and urgent identification of new drug targets for treatment of 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 comprises a single RNA of about 30 kb in length, in which 14 open reading frames (ORFs) have been annotated, and encodes approximately 30 proteins. The first two-thirds of the SARS-CoV-2 genome is made up of two large overlapping open-reading-frames (ORF1a and ORF1b) encoding a replicase polyprotein, which is subsequently cleaved to yield 16 so-called non-structural proteins. The non-structural protein 1 (Nsp1), which is considered to be a major virulence factor, suppresses host immune functions by associating with host ribosomal complexes at the very end of its C-terminus. Furthermore, Nsp1 facilitates initiation of viral RNA translation via an interaction of its N-terminal domain with the 5′ untranslated region (UTR) of the viral RNA. Here, we report the near-complete backbone chemical-shift assignments of full-length SARS-CoV-2 Nsp1 (19.8 kDa), which reveal the domain organization, secondary structure and backbone dynamics of Nsp1, and which will be of value to further NMR-based investigations of both the biochemical and physiological functions of Nsp1.
KW - 5′ untranslated region
KW - New drug targets
KW - NMR spectroscopy
KW - Non-structural proteins
KW - Nsp1
KW - SARS-CoV-2
UR - http://www.scopus.com/inward/record.url?scp=85103119352&partnerID=8YFLogxK
U2 - 10.1007/s12104-021-10019-6
DO - 10.1007/s12104-021-10019-6
M3 - Article
C2 - 33770349
AN - SCOPUS:85103119352
VL - 15
SP - 287
EP - 295
JO - Biomolecular NMR assignments
JF - Biomolecular NMR assignments
SN - 1874-2718
IS - 2
ER -