Host: E. coli • AA: 1-527 (full length) • Tag: N-terminal GST • MW: 86.3 kDa
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SARS-CoV-2 nsp14 Methyltransferase (recombinant)

Item No. 40884

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • SARS-CoV-2 Guanine-N7 Methyltransferase
  • SARS-CoV-2 Guanine-N7 MTase
  • SARS-CoV-2 Non-structural Protein 14
  • Severe Acute Respiratory Syndrome Coronavirus 2 nsp14 Methyltransferase
Purity
≥90% estimated by SDS-PAGE
Endotoxin Testing
<1.0 EU/µg determined by the LAL endotoxin assay
Source
Recombinant SARS-CoV-2 N-terminal GST-tagged nsp14 expressed in E. coli
Amino Acids
1-527
Formulation (Request formulation change)
50 mM Tris, pH 7.5, with 200 mM sodium chloride and 20% glycerol
UniProt Accession №
P0DTD1
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    100 µg

    $601

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    500 µg

    $1,947

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    Product Description

    Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is an enveloped positive-stranded RNA virus and the causative agent of COVID-19, a primarily respiratory illness characterized by fever, cough, and shortness of breath that can lead to life-threatening complications.1,2,3,4,5 The SARS-CoV-2 genome contains approximately 30 kilobases and 14 open reading frames (ORFs) that encode four structural proteins: spike, envelope, membrane, and nucleocapsid, as well as 16 non-structural proteins and 9 accessory factors.6 SARS-CoV-2 non-structural protein 14 (nsp14), also known as guanine-N7 methyltransferase (guanine-N7 MTase), is encoded within ORF1ab with an amino acid sequence that displays few mutations and is highly conserved across coronaviruses and SARS-CoV-2 variants.6,7,8 It is a bifunctional enzyme having an N-terminal exoribonuclease domain (ExoN domain) and a C-terminal methyltransferase domain.6,7 SARS-CoV-2 nsp14 forms an exonuclease complex with the cofactor nsp10, which binds to and stabilizes the disordered ExoN domain and is a necessary interaction for accurate exoribonuclease and RNA strand proofreading activities.8,6,7 It also forms a ternary methylation complex with nsp10 and nsp16 methyltransferase, also known as 2ʹ-O-methyltransferase (2ʹ-O-MTase), and catalyzes guanosine methylation in the viral mRNA 5ʹ-end cap prior to the terminal ribose methylation catalyzed by 2ʹ-O-MTase.6,9 SARS-CoV-2 nsp14 inhibits IFN-β reporter gene activation induced by the retinoic acid-inducible gene I caspase activation and recruitment domain (RIG-I 2CARD domain) in HEK293FT cells, as well as inhibits global protein translation and expression of IFN-stimulated genes (ISGs) in HEK293T cells expressing SARS-CoV-2 nsp14.10,7

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Kandeel, M., Ibrahim, A., Fayez, M., et al. From SARS and MERS CoVs to SARS-CoV-2: Moving toward more biased codon usage in viral structural and nonstructural genes. J. Med. Virol. 92(6), 660-666 (2020).

    2. Lu, R., Zhao, X., Li, J., et al. Genomic characterisation and epidemiology of 2019 novel coronavirus: Implications for virus origins and receptor binding. Lancet 395(10224), 565-574 (2020).

    3. Meo, S.A., Alhowikan, A.M., Al-Khlaiwi, T., et al. Novel coronavirus 2019-nCoV: Prevalence, biological and clinical characteristics comparison with SARS-CoV and MERS-CoV. Eur. Rev. Med. Pharmacol. Sci. 24(4), 2012-2019 (2020).

    4. Klok, F.A., Kruip, M.J.H.A., van der Meer, N.J.M., et al. Incidence of thrombotic complications in critically ill ICU patients with COVID-19. Thromb. Res. 191, 145-147 (2020).

    5. Yang, F., Shi, S., Zhu, J., et al. Analysis of 92 deceased patients with COVID-19. J. Med. Virol. 92(11), 2511-2515 (2020).

    6. Romano, M., Ruggiero, A., Squeglia, F., et al. A structural view of SARS-CoV-2 RNA replication machinery: RNA synthesis, proofreading and final capping. Cells 9(5), 1267 (2020).

    7. Hsu, J.C.-C., Laurent-Rolle, M., Pawlak, J.B., et al. Translational shutdown and evasion of the innate immune response by SARS-CoV-2 NSP14 protein. Proc. Natl. Acad. Sci. USA 118(24), e2101161118 (2021).

    8. Wang, X., Tao, C., Morozova, I., et al. Identifying structural features of nucleotide analogues to overcome SARS-CoV-2 exonuclease activity. Viruses 14(7), 1413 (2022).

    9. Viswanathan, T., Arya, S., Chan, S.-H., et al. Structural basis of RNA cap modification by SARS-CoV-2. Nat. Commun. 11(1), 3718 (2020).

    10. Yuen, C.-K., Lam, J.-Y., Wong, W.-M., et al. SARS-CoV-2 nsp13, nsp14, nsp15 and orf6 function as potent interferon antagonists. Emerg. Microbes Infect. 9(1), 1418-1428 (2020).