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Related Experiment Video

Updated: Jun 30, 2026

Screening for Functional Non-coding Genetic Variants Using Electrophoretic Mobility Shift Assay EMSA and DNA-affinity Precipitation Assay DAPA

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Monitoring SARS-CoV-2 Nsp13 helicase binding activity using expanded genetic code techniques.

Eryn Lundrigan¹, Christine Hum¹, Nadine Ahmed¹

¹Department of Chemistry and Biomolecular Sciences, University of Ottawa Ottawa Ontario K1N 6N5 Canada john.pezacki@uottawa.ca.

RSC Chemical Biology

|May 1, 2025

Summary

This summary is machine-generated.

Researchers developed a new method to study the SARS-CoV-2 Nsp13 helicase using fluorescent labeling. This technique helps understand enzyme activity and could lead to new pan-coronavirus therapies.

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Area of Science:

Biochemistry
Molecular Biology
Virology

Background:

The SARS-CoV-2 Nsp13 helicase is crucial for viral replication and a potential target for broad-spectrum coronavirus treatments.
Understanding its binding and unwinding mechanisms is key to developing effective therapeutics.

Purpose of the Study:

To develop a method for site-specific fluorescent labeling of the Nsp13 helicase using non-canonical amino acids.
To investigate the enzyme's substrate binding and translocation dynamics using Förster resonance energy transfer (FRET).

Main Methods:

Genetic code expansion was used to incorporate *p*-azido-l-phenylalanine (AzF) into Nsp13 at five specific sites.
The resulting Nsp13-AzF was labeled with a Cy5 fluorophore.
FRET assays were employed to monitor enzyme-substrate interactions and translocation.

Main Results:

Site-specific incorporation of AzF and Cy5 labeling did not impede Nsp13 helicase activity.
FRET-based assays successfully monitored the binding dynamics of labeled Nsp13 constructs to nucleic acid substrates.
The study demonstrated distance-dependent binding interactions.

Conclusions:

This approach enables direct monitoring of Nsp13 helicase binding activity.
The method offers a novel platform for screening inhibitors of this essential viral enzyme.
This research contributes to the development of potential pan-coronavirus therapeutics.