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Related Experiment Video

Updated: Jun 6, 2025

Production of Pseudotyped Particles to Study Highly Pathogenic Coronaviruses in a Biosafety Level 2 Setting

Production of Pseudotyped Particles to Study Highly Pathogenic Coronaviruses in a Biosafety Level 2 Setting

Published on: March 1, 2019

Direct lipid interactions control SARS-CoV-2 M protein conformational dynamics and virus assembly.

Mandira Dutta¹, Kimberly A Dolan², Souad Amiar³

¹Department of Chemistry, The University of Chicago, Chicago, IL 60637.

Biorxiv : the Preprint Server for Biology

|November 22, 2024

Summary

Coronaviruses

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Engineering Antiviral Agents via Surface Plasmon Resonance

Engineering Antiviral Agents via Surface Plasmon Resonance

Published on: June 14, 2022

Area of Science:

Virology
Structural Biology
Biochemistry

Background:

The SARS-CoV-2 M protein is crucial for infectious virus particle formation.
M protein exists in two conformations (M_short and M_long), with transitions potentially regulating viral assembly.

Purpose of the Study:

To identify factors regulating M protein conformation and the roles of each state.
To elucidate the interaction between M protein and sphingolipids.

Main Methods:

Molecular dynamics simulations to study M protein conformational changes.
Cryo-electron microscopy (Cryo-EM) to determine M protein structure.
Biochemical assays to assess M protein interactions and function.

Main Results:

Discovered a direct interaction between M protein and Golgi-enriched anionic lipids, specifically ceramide-1-phosphate (C1P).
C1P binding stabilizes the M_short conformation and promotes a transition from M_long to M_short.
Cryo-EM revealed C1P binds to a conserved site on M_short.
Disruption of the M_short-C1P interaction impaired viral assembly, reduced interactions with Spike and E proteins, and compromised virus-like particle entry.

Conclusions:

Endogenous signaling lipids, like C1P, directly regulate M protein structure and dynamics.
M_short conformation is stabilized by C1P in the early endomembrane system, facilitating the organization of structural proteins for viral budding.