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Modeling The Lifecycle Of Ebola Virus Under Biosafety Level 2 Conditions With Virus-like Particles Containing Tetracistronic Minigenomes
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Ebola Virus Matrix Protein VP40 Single Mutations G198R and G201R Significantly Enhance Plasma Membrane Localization.

Michael D Cioffi1, Tej Sharma1, Balindile B Motsa2

  • 1Department of Physics, Florida International University, Miami, Florida 33199, United States.

The Journal of Physical Chemistry. B
|September 26, 2024
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Summary

Ebola virus matrix protein VP40 mutations G198R and G201R enhance viral assembly by altering interactions with the host cell membrane. Molecular dynamics simulations reveal how these mutations facilitate deeper membrane penetration and improved viral budding.

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Area of Science:

  • Virology
  • Molecular Biology
  • Biophysics

Background:

  • Ebola virus matrix protein VP40 is crucial for viral envelope formation and assembly.
  • Mutations in VP40 can alter its interaction with the host cell plasma membrane (PM), affecting viral budding.
  • Specific mutations, G198R and G201R, were previously shown to enhance VP40 assembly and virus-like particle budding.

Purpose of the Study:

  • To investigate the molecular mechanisms by which VP40 mutations G198R and G201R influence plasma membrane localization and interactions.
  • To understand how these mutations affect the binding orientation and membrane penetration of VP40.
  • To elucidate the role of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) in mediating the effects of VP40 mutations.

Main Methods:

  • Multiscale molecular dynamics (MD) simulations, including all-atom and coarse-grained approaches.
  • Simulations were performed using a dimer-dimer configuration of VP40, focusing on the C-terminal domain (CTD).
  • Analysis of VP40-membrane interactions, including binding orientation, membrane penetration, and specific residue interactions.

Main Results:

  • Mutations on the outer surface of VP40's CTD alter its membrane binding orientation and increase membrane penetration.
  • Direct interactions between PI(4,5)P2 and mutated residues stabilize VP40 binding and enhance its pull into the PM.
  • Mutations increase accessibility to otherwise inaccessible amino acids, promoting stronger VP40-PM interactions.

Conclusions:

  • Single amino acid mutations in VP40 can significantly alter its plasma membrane interactions at a molecular level.
  • These alterations, particularly enhanced membrane binding and penetration, contribute to increased viral assembly and budding.
  • Understanding these mutation-driven mechanisms is vital for mitigating Ebola virus disease severity and predicting outbreaks.