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Function
The non-structural protein nsp9 contains 113 amino acids[1] and is encoded on the ORF1a[2].
The SARS-CoV nsp9 has been shown to bind to RNA and DNA but preferably to ssRNA and may interact with the replication complex (consisting of nsp7, nsp8 and nsp12). The SARS-CoV-2 nsp9 interactome suggests various potential functions in viral replication, regulating nuclear transport, inhibition of host cell transcription, host shut off or as a complicating factor during pathogenesis[3].
Disease
The global COVID-19 pandemic, which started in 2019, is caused by the SARS-CoV-2.
Structure
The protein structure has an unusual fold, so far only found within coronaviruses. It consists of seven β-sheets and one α-helix at the C-terminus. The β1-β7 fold to form a β-barrel structure. Half of β7 additionally forms a twisted β-hairpin with β6, interacting with the C-terminus. The extended loops connecting the β-strands are directed outward, of which β2-3 and β3-4 are glycine rich, positively charged and might play a role in RNA binding. The conserved GxxxG motif is important for the forming of a nsp9 homodimer[4].
Nsp9 has been shown to be able to bind to rhinoviral 3C protease sequence (LEVL) close to the dimer binding site[4].
Variations
Compared to the amino acid sequence of SARS-CoV, the SARS-CoV-2 sequence of nsp9 has three amino acid substitutions, resulting in a sequence identity of 97.3%[1].
See also
Coronavirus_Disease 2019 (COVID-19)
SARS-CoV-2_virus_proteins
COVID-19 AlphaFold2 Models
- ↑ 1.0 1.1 Yoshimoto FK. The Proteins of Severe Acute Respiratory Syndrome Coronavirus-2 (SARS CoV-2 or n-COV19), the Cause of COVID-19. Protein J. 2020 Jun;39(3):198-216. doi: 10.1007/s10930-020-09901-4. PMID:32447571 doi:https://dx.doi.org/10.1007/s10930-020-09901-4
- ↑ Konkolova E, Klima M, Nencka R, Boura E. Structural analysis of the putative SARS-CoV-2 primase complex. J Struct Biol. 2020 Aug 1;211(2):107548. doi: 10.1016/j.jsb.2020.107548. Epub, 2020 Jun 11. PMID:32535228 doi:https://dx.doi.org/10.1016/j.jsb.2020.107548
- ↑ Gordon DE, Jang GM, Bouhaddou M, Xu J, Obernier K, White KM, O'Meara MJ, Rezelj VV, Guo JZ, Swaney DL, Tummino TA, Huttenhain R, Kaake RM, Richards AL, Tutuncuoglu B, Foussard H, Batra J, Haas K, Modak M, Kim M, Haas P, Polacco BJ, Braberg H, Fabius JM, Eckhardt M, Soucheray M, Bennett MJ, Cakir M, McGregor MJ, Li Q, Meyer B, Roesch F, Vallet T, Mac Kain A, Miorin L, Moreno E, Naing ZZC, Zhou Y, Peng S, Shi Y, Zhang Z, Shen W, Kirby IT, Melnyk JE, Chorba JS, Lou K, Dai SA, Barrio-Hernandez I, Memon D, Hernandez-Armenta C, Lyu J, Mathy CJP, Perica T, Pilla KB, Ganesan SJ, Saltzberg DJ, Rakesh R, Liu X, Rosenthal SB, Calviello L, Venkataramanan S, Liboy-Lugo J, Lin Y, Huang XP, Liu Y, Wankowicz SA, Bohn M, Safari M, Ugur FS, Koh C, Savar NS, Tran QD, Shengjuler D, Fletcher SJ, O'Neal MC, Cai Y, Chang JCJ, Broadhurst DJ, Klippsten S, Sharp PP, Wenzell NA, Kuzuoglu-Ozturk D, Wang HY, Trenker R, Young JM, Cavero DA, Hiatt J, Roth TL, Rathore U, Subramanian A, Noack J, Hubert M, Stroud RM, Frankel AD, Rosenberg OS, Verba KA, Agard DA, Ott M, Emerman M, Jura N, von Zastrow M, Verdin E, Ashworth A, Schwartz O, d'Enfert C, Mukherjee S, Jacobson M, Malik HS, Fujimori DG, Ideker T, Craik CS, Floor SN, Fraser JS, Gross JD, Sali A, Roth BL, Ruggero D, Taunton J, Kortemme T, Beltrao P, Vignuzzi M, Garcia-Sastre A, Shokat KM, Shoichet BK, Krogan NJ. A SARS-CoV-2 protein interaction map reveals targets for drug repurposing. Nature. 2020 Jul;583(7816):459-468. doi: 10.1038/s41586-020-2286-9. Epub 2020 Apr, 30. PMID:32353859 doi:https://dx.doi.org/10.1038/s41586-020-2286-9
- ↑ 4.0 4.1 Littler DR, Gully BS, Colson RN, Rossjohn J. Crystal Structure of the SARS-CoV-2 Non-structural Protein 9, Nsp9. iScience. 2020 Jul 24;23(7):101258. doi: 10.1016/j.isci.2020.101258. Epub 2020, Jun 9. PMID:32592996 doi:https://dx.doi.org/10.1016/j.isci.2020.101258
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