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TitleRemdesivir overcomes the S861 roadblock in SARS-CoV-2 polymerase elongation complex.
Journal, issue, pagesCell Rep, Vol. 37, Issue 4, Page 109882, Year 2021
Publish dateOct 26, 2021
AuthorsJiqin Wu / Haofeng Wang / Qiaojie Liu / Rui Li / Yan Gao / Xiang Fang / Yao Zhong / Meihua Wang / Quan Wang / Zihe Rao / Peng Gong /
PubMed AbstractRemdesivir (RDV), a nucleotide analog with broad-spectrum features, has exhibited effectiveness in COVID-19 treatment. However, the precise working mechanism of RDV when targeting the viral RNA- ...Remdesivir (RDV), a nucleotide analog with broad-spectrum features, has exhibited effectiveness in COVID-19 treatment. However, the precise working mechanism of RDV when targeting the viral RNA-dependent RNA polymerase (RdRP) has not been fully elucidated. Here, we solve a 3.0-Å structure of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) RdRP elongation complex (EC) and assess RDV intervention in polymerase elongation phase. Although RDV could induce an "i+3" delayed termination in meta-stable complexes, only pausing and subsequent elongation are observed in the EC. A comparative investigation using an enterovirus RdRP further confirms similar delayed intervention and demonstrates that steric hindrance of the RDV-characteristic 1'-cyano at the -4 position is responsible for the "i+3" intervention, although two representative Flaviviridae RdRPs do not exhibit similar behavior. A comparison of representative viral RdRP catalytic complex structures indicates that the product RNA backbone encounters highly conserved structural elements, highlighting the broad-spectrum intervention potential of 1'-modified nucleotide analogs in anti-RNA virus drug development.
External linksCell Rep / PubMed:34653416 / PubMed Central
MethodsEM (single particle)
Resolution3.0 Å
Structure data

30852

7dte

EMDB-30852, PDB-7dte:
SARS-CoV-2 RdRP catalytic complex with T33-1 RNA
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • severe acute respiratory syndrome coronavirus 2
  • foot-and-mouth disease virus
KeywordsVIRAL PROTEIN/RNA / COVID-19 / SARS-CoV-2 / Virus / RdRp / nsp12 / nsp7 / nsp8 / RTC / cryo-EM / Viral protein / RNA polymerase / drug target / antiviral / VIRAL PROTEIN-RNA complex

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