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Updated: Jun 16, 2025
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Engineering Antiviral Agents via Surface Plasmon Resonance
Published on: June 14, 2022
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Structural adaptability of SARS-CoV-2 Nsp1 with the host network.
Monikaben Padariya1, Ted Hupp2,3, Umesh Kalathiya4
1International Centre for Cancer Vaccine Science, University of Gdansk, Ul. Kładki 24, 80-822, Gdansk, Poland. monikaben.padariya@ug.edu.pl.
European Biophysics Journal : EBJ
|June 14, 2025
Summary
The SARS-CoV-2 non-structural protein 1 (Nsp1) binds the 40S ribosome and cyclophilins. Computational analysis revealed Nsp1’s versatile C-terminus is key for these interactions, aiding drug discovery for coronaviruses.
Area of Science:
- Structural biology
- Virology
- Computational chemistry
Background:
- Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) non-structural protein 1 (Nsp1) is crucial for viral replication.
- Nsp1 inhibits host cell translation by binding the 40S ribosomal subunit and interacting with cyclophilins.
Purpose of the Study:
- To investigate the structural and physicochemical properties of SARS-CoV-2 Nsp1.
- To understand Nsp1's interactions with the 40S ribosome and cyclophilins using computational methods.
Main Methods:
- Computational techniques were employed to analyze SARS-CoV-2 Nsp1 structure.
- Pharmacophores for Nsp1-ribosome (uS3, eS30) and Nsp1-cyclophilin interactions were constructed.
Main Results:
- SARS-CoV-2 Nsp1 possesses a structured α-helical C-terminus, with a conformational switch at S166 essential for 40S ribosome binding.
- Cyclophilins stabilize the Nsp1 C-terminus, inducing a tilt at residue 166.
- FKBP1B exhibited the highest affinity for Nsp1, while PPIH showed minimal interaction.
Conclusions:
- Nsp1 features a versatile C-terminus that adapts its conformation based on the binding partner.
- Novel Nsp1 binding sites were identified, offering potential for developing therapeutics against coronaviruses.
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