Characterization of the guanine-N7 methyltransferase activity of coronavirus nsp14 on nucleotide GTP

Xu Jin, Yu Chen, Ying Sun, Cong Zeng, Yi Wang, Jiali Tao, Andong Wu, Xiao Yu, Zhou Zhang, Jie Tian, Deyin Guo*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

40 Scopus citations


Most eukaryotic viruses that replicate in the cytoplasm, including coronaviruses, have evolved strategies to cap their RNAs. In our previous work, the nonstructural protein (nsp) 14 of severe acute respiratory syndrome coronavirus (SARS-CoV) was identified as a cap (guanine-N7)-methyltransferase (N7-MTase). In this study, we found that GTP, dGTP as well as cap analogs GpppG, GpppA and m7GpppG could be methylated by SARS-CoV nsp14. In contrast, the nsp14 could not modify ATP, CTP, UTP, dATP, dCTP, dUTP or cap analog m7GpppA. Critical residues of nsp14 essential for the methyltransferase activity on GTP were identified, which include F73, R84, W86, R310, D331, G333, P335, Y368, C414, and C416. We further showed that the methyltransferase activity of GTP was universal for nsp14 of other coronaviruses. Moreover, the accumulation of m7GTP or presence of protein nsp14 could interfere with protein translation of cellular mRNAs. Altogether, the results revealed a new enzymatic activity of coronavirus nsp14.

Original languageEnglish (US)
Pages (from-to)45-52
Number of pages8
JournalVirus Research
Issue number1-2
StatePublished - Sep 2013
Externally publishedYes


  • Coronavirus
  • GTP methylation
  • Nsp14
  • SARS
  • Translation

ASJC Scopus subject areas

  • Virology
  • Infectious Diseases
  • Cancer Research


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