SARS-CoV-2 nsp16 Methyltransferase (recombinant)

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 nsp16 methyltransferase (recombinant) is a 2'-O-methyltransferase (2'-O-MTase) and has a role in 5'-end capping of viral mRNAs.^7,8 In coronaviruses, nsp16 forms a complex with nsp10 to methylate nascent mRNAs at the ribose 2'-O position, creating a Cap-1 structure that facilitates increased translation of viral mRNAs and reduced innate immune recognition by the host cell.^8,9 Deficiency of nsp16 in the related virus SARS-CoV reduces viral RNA synthesis by approximately 10-fold in vitro, and mutations in the nsp16 KDKE catalytic tetrad in mouse-adapted SARS-CoV attenuate the virus in vivo.^8,10 An nsp10-derived peptide inhibitor of the nsp16/nsp10 complex increases survival in a mouse model of infection with the coronavirus mouse hepatitis virus (MHV).⁹ Cayman's SARS-CoV-2 nsp16 Methyltransferase (recombinant) protein consists of 299 amino acids and has a calculated molecular weight of 33.46 kDa.

WARNING This product is not for human or veterinary use.

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. Krafcikova, P., Silhan, J., Nancka, R., et al. Structural analysis of the SARS-CoV-2 methyltransferase complex involved in RNA cap creation bound to sinefungin. Nat. Commun. 11(1), 3717 (2020).

8. 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).

9. Wang, Y., Sun, Y., Wu, A., et al. Coronavirus nsp10/nsp16 methyltransferase can be targeted by nsp10-derived peptide in vitro and in vivo to reduce replication and pathogenesis. J. Virol. 89(16), 8416-8427 (2015).

10. Menachery, V.D., Yount, B.L.J., Josset, L., et al. Attenuation and restoration of severe acute respiratory syndrome coronavirus mutant lacking 2'-O-methyltransferase activity. J. Virol. 88(8), 4251-4264 (2014).