Understanding the Activated Form of a Class-I Fusion Protein: Modeling the Interaction of the Ebola Virus Glycoprotein 2 with a Lipid Bilayer
- 22 September 2020
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 59 (41), 4051-4058
- https://doi.org/10.1021/acs.biochem.0c00527
Abstract
Fusion of the viral and target cell membranes is a key step in the life cycle of all enveloped viruses. Here, a range of structural data is used to generate an evidence-based model of the active conformation of an archetypical type-I fusion protein, the Ebola glycoprotein 2 (GP2). The stability of the trimeric complex is demonstrated using molecular dynamics and validated by simulating the interaction of the complex with a lipid bilayer. In this model the fusion peptides project away from the central helix bundle parallel to the target membrane. This maximizes contact with the host membrane, enhances lateral stability and would explain why, when activated, viral fusion proteins are trimeric.Keywords
Funding Information
- Department of Education and Training (DP160103414, DP180101421)
This publication has 46 references indexed in Scilit:
- Cryo-EM analysis of the post-fusion structure of the SARS-CoV spike glycoproteinNature Communications, 2020
- Structural transitions in influenza haemagglutinin at membrane fusion pHNature, 2020
- Tick-Borne Encephalitis Virus: A Structural ViewViruses, 2018
- Structure and stabilization of the Hendra virus F glycoprotein in its prefusion formProceedings of the National Academy of Sciences of the United States of America, 2015
- Herpesvirus gB: A Finely Tuned Fusion MachineViruses, 2015
- Composition and Functions of the Influenza Fusion PeptideProtein & Peptide Letters, 2009
- Structure of the Ebola virus glycoprotein bound to an antibody from a human survivorNature, 2008
- Structures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeCritical Reviews in Biochemistry and Molecular Biology, 2008
- Structure of the dengue virus envelope protein after membrane fusionNature, 2004
- Characteristics of Filoviridae: Marburg and Ebola VirusesThe Science of Nature, 1999