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TitleMolecular basis of SARS-CoV-2 proofreading enzyme-mediated resistance to remdesivir.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 122, Issue 40, Page e2519755122, Year 2025
Publish dateOct 7, 2025
AuthorsYang Yang / Yu Li / Scott T Becker / Ayesha Khan / Gloria Luo / Bin Liu / Chang Liu /
PubMed AbstractSARS-CoV-2's remarkable resistance to nucleotide analog antivirals such as remdesivir, which thwarts RNA synthesis by inhibiting viral polymerase (RdRp), challenges available therapies. We reveal ...SARS-CoV-2's remarkable resistance to nucleotide analog antivirals such as remdesivir, which thwarts RNA synthesis by inhibiting viral polymerase (RdRp), challenges available therapies. We reveal that remdesivir incorporation destabilizes RdRp-RNA complex while enhancing RNA binding to the proofreading exoribonuclease (ExoN), facilitating remdesivir excision. Conserved ExoN determinants for remdesivir recognition and excision underpin ExoN-mediated resistance across all coronaviruses. These findings inform the design of next-generation antivirals and combination therapies capable of overcoming ExoN-mediated resistance.
External linksProc Natl Acad Sci U S A / PubMed:41032524 / PubMed Central
MethodsEM (single particle)
Resolution2.81 Å
Structure data

72127

9q1j

EMDB-72127, PDB-9q1j:
Cryo-EM structure of SARS-CoV-2 nsp10-nsp14 E191A mutant-T20P14-R complex
Method: EM (single particle) / Resolution: 2.81 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

Source
  • severe acute respiratory syndrome coronavirus 2
KeywordsVIRAL PROTEIN / SARS-CoV-2 / replication and transcription / mismatch / proofreading exoribonuclease / VIRAL PROTEIN-RNA complex

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