The Energetics of Membrane Fusion from Binding, through Hemifusion, Pore Formation, and Pore Enlargement
- 1 May 2004
- journal article
- review article
- Published by Springer Nature in The Journal of Membrane Biology
- Vol. 199 (1) , 1-14
- https://doi.org/10.1007/s00232-004-0669-8
Abstract
The main steps of viral membrane fusion are local membrane approach, hemifusion, pore formation, and pore enlargement. Experiments and theoretical analyses have helped determine the relative energies required for each step. Key protein structures and conformational changes of the fusion process have been identified. The physical deformations of monolayer bending and lipid tilt have been applied to the steps of membrane fusion. Experiment and theory converge to strongly indicate that, contrary to former conceptions, the fusion process is progressively more energetically difficult: hemifusion has a relatively low energy barrier, pore formation is more energy-consuming, and pore enlargement is the most difficult to achieve.Keywords
This publication has 128 references indexed in Scilit:
- Conformational change and protein–protein interactions of the fusion protein of Semliki Forest virusNature, 2004
- The structural biology of type I viral membrane fusionNature Reviews Molecular Cell Biology, 2003
- Membrane FusionCell, 2003
- Observation of a Membrane Fusion Intermediate StructureScience, 2002
- A quantitative model for membrane fusion based on low-energy intermediatesProceedings of the National Academy of Sciences, 2001
- Restricted movement of lipid and aqueous dyes through pores formed by influenza hemagglutinin during cell fusion.The Journal of cell biology, 1994
- Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection.Proceedings of the National Academy of Sciences, 1994
- Structure of influenza haemagglutinin at the pH of membrane fusionNature, 1994
- A spring-loaded mechanism for the conformational change of influenza hemagglutininCell, 1993
- Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolutionNature, 1981