AVITHRAPID

Part of EU Open Research Repository
Published July 16, 2025 | Version v1
Poster Open

Optimization and Validation of a Biochemical Fret Assay For the Exonuclease Activity of SARS CoV-2 nsp14-nsp10 Complex

Creators

  • 1. ROR icon University of Cagliari

Description

SARS-CoV-2, the virus responsible for COVID-19, has one of the longest RNA genomes among RNA viruses. To correct replication errors, it uses a unique proofreading mechanism involving the nsp14 protein, which has 3'-5' exonuclease activity, assisted by the cofactor nsp10. Currently, there are no drugs targeting this function. To support antiviral research, nsp14 and nsp10 were expressed and purified in E. Coli cells, and a FRET-based biochemical assay was developed to study their exonuclease activity, as previously mentioned in the literature. This system lays the groundwork for identifying future inhibitors of the nsp14-nsp10 complex.

Files

Poster DETTORI LAURA SIV ISV.pdf

Files (750.7 kB)

Name Size Download all
md5:d4b8eec12cfdd8d426bfb7c2be7ed07e
750.7 kB Preview Download

Additional details

Identifiers

Other
Poster

Related works

Is original form of
Poster: Poster (Other)

Funding

European Commission
AVITHRAPID - Antiviral Therapeutics for Rapid Response Against Pandemic Infectious Diseases 101137192

Dates

Other
2025-06-22
Poster

References

  • Rona G, Zeke A et al. The NSP14/NSP10 RNA repair complex as a Pan-coronavirus therapeutic target. Cell Death Differ. 2022 Feb;29(2):285-292
  • Asthana, A.; Corona, A.; et al. Analogs of the Catechol Derivative Dynasore Inhibit HIV-1 Ribonuclease H, SARS-CoV-2 nsp14 Exoribonuclease, and Virus Replication. Viruses 2023, 15, 1539