SARS-CoV-2 Nucleoprotein

Target not currently curated in GtoImmuPdb

Target id: 3121

Nomenclature: SARS-CoV-2 Nucleoprotein

Annotation status: Awaiting annotation/under development. Please contact us if you can help with annotation. » Email us

Gene and Protein Information
Species	TM	AA	Chromosomal Location	Gene Symbol	Gene Name	Reference
SARS-CoV-2	-	419		N

Previous and Unofficial Names
nucleocapsid phosphoprotein

Database Links
Entrez Gene
RefSeq Protein
UniProtKB	P0DTC9 (CoV2)

General Comments
The coronavirus nucleocapsid phosphoprotein (N, or nucleoprotein) is highly basic and binds the viral RNA as a dimeric entity [1] into nucleocapsids which protect the viral genome, while also providing access for replication when required. Of three targets suggested to associate with SARS-CoV-2 N phosphoprotein (in a cell-free system [2], in preprint form), G3BP1 (G3BP stress granule assembly factor 1; UniProt accession Q13283) seems a relevant focus for therapy against COVID-19. G3BP1 regulates the innate immune response [3-4,6-7] and stress granules reduce the replication of MERS-CoV [5], so there is potential here for targetted drug discovery.

The coronavirus nucleocapsid phosphoprotein (N, or nucleoprotein) is highly basic and binds the viral RNA as a dimeric entity [1] into nucleocapsids which protect the viral genome, while also providing access for replication when required. Of three targets suggested to associate with SARS-CoV-2 N phosphoprotein (in a cell-free system [2], in preprint form), G3BP1 (G3BP stress granule assembly factor 1; UniProt accession Q13283) seems a relevant focus for therapy against COVID-19. G3BP1 regulates the innate immune response [3-4,6-7] and stress granules reduce the replication of MERS-CoV [5], so there is potential here for targetted drug discovery.

References

Show »« Hide

1. Fan H, Ooi A, Tan YW, Wang S, Fang S, Liu DX, Lescar J. (2005) The nucleocapsid protein of coronavirus infectious bronchitis virus: crystal structure of its N-terminal domain and multimerization properties. Structure, 13 (12): 1859-68. [PMID:16338414]

2. Gordon DE, Jang GM, Bouhaddou M, Xu J, Obernier K, White KM, O'Meara MJ, Rezelj VV, Guo JZ, Swaney DL et al.. (2020) A SARS-CoV-2 protein interaction map reveals targets for drug repurposing. Nature, [Epub ahead of print]. [PMID:32353859]

3. Kim SS, Sze L, Liu C, Lam KP. (2019) The stress granule protein G3BP1 binds viral dsRNA and RIG-I to enhance interferon-β response. J. Biol. Chem., 294 (16): 6430-6438. [PMID:30804210]

4. Liu ZS, Cai H, Xue W, Wang M, Xia T, Li WJ, Xing JQ, Zhao M, Huang YJ, Chen S et al.. (2019) G3BP1 promotes DNA binding and activation of cGAS. Nat. Immunol., 20 (1): 18-28. [PMID:30510222]

5. Nakagawa K, Narayanan K, Wada M, Makino S. (2018) Inhibition of Stress Granule Formation by Middle East Respiratory Syndrome Coronavirus 4a Accessory Protein Facilitates Viral Translation, Leading to Efficient Virus Replication. J. Virol., 92 (20). [PMID:30068649]

6. Wiser C, Kim B, Ascano M. (2019) G3BP1 enhances cytoplasmic DNA pattern recognition. Nat. Immunol., 20 (1): 5-7. [PMID:30538338]

7. Yang W, Ru Y, Ren J, Bai J, Wei J, Fu S, Liu X, Li D, Zheng H. (2019) G3BP1 inhibits RNA virus replication by positively regulating RIG-I-mediated cellular antiviral response. Cell Death Dis, 10 (12): 946. [PMID:31827077]

How to cite this page

Select citation format:

SARS-CoV-2 Nucleoprotein

Contents:

References

How to cite this page