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The SARS-CoV-2 nucleoprotein associates with anionic lipid membranes
Mandira Dutta1, Yuan Su2, Gregory A Voth1
1Department of Chemistry, Chicago Center for Theoretical Chemistry, Institute for Biophysical Dynamics, and James Frank Institute, The University of Chicago, Chicago, IL, USA.
Biorxiv : the Preprint Server for Biology
|September 25, 2023
Summary
The SARS-CoV-2 nucleoprotein (N) binds anionic lipids via its C-terminal domain. This interaction is crucial for recruiting N to M protein assembly sites, facilitating new virus particle formation.
Area of Science:
- Virology
- Molecular Biology
- Biochemistry
Background:
- Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a lipid-enveloped virus responsible for the COVID-19 pandemic.
- Viral assembly and budding, critical for SARS-CoV-2 replication, involve structural proteins like the nucleoprotein (N).
- The precise mechanisms by which SARS-CoV-2 acquires its lipid bilayer and assembles new virions remain incompletely understood.
Conclusions:
- A lipid-dependent model for the recruitment of the SARS-CoV-2 N protein to M protein assembly sites is proposed.
- This model integrates in vitro, cellular, and in silico data to explain a critical step in viral lifecycle.
- Understanding N protein-lipid interactions provides insights into SARS-CoV-2 assembly and potential therapeutic targets.
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