1-palmitoyl-2-oleoylglycero-3-phosphoserine and Hemorrhagic-Fever--Ebola

The Ebola virus matrix protein VP40 is a major structural protein that provides the scaffolding for new Ebola virus particles. For this, VP40 is first trafficked to the lower leaflet of the plasma membrane (PM) in its dimeric form. Once associated with the PM, the VP40 dimers undergo structural rearrangements and oligomerize into hexamers and filaments that make up the virus matrix. Therefore, association of the VP40 dimers and their stabilization at the PM is a crucial step in the Ebola life-cycle. To understand the molecular details of the VP40 dimer-PM interactions, we investigated the dimer association with the inner leaflet of the PM using detailed all-atom molecular dynamics (MD) simulations. The formation of the dimer-PM complex is facilitated by the interactions of the VP40 lysine residues and the anionic lipids POPS, POPI, and PIP

Topics: Anions; Cell Membrane; Ebolavirus; Hemorrhagic Fever, Ebola; Hydrophobic and Hydrophilic Interactions; Lipid Bilayers; Lipids; Molecular Dynamics Simulation; Nucleoproteins; Phosphatidylserines; Protein Conformation, alpha-Helical; Protein Multimerization; Viral Core Proteins; Virus Release