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Title: Viral membrane fusion

Abstract

Membrane fusion is an essential step when enveloped viruses enter cells. Lipid bilayer fusion requires catalysis to overcome a high kinetic barrier; viral fusion proteins are the agents that fulfill this catalytic function. Despite a variety of molecular architectures, these proteins facilitate fusion by essentially the same generic mechanism. Stimulated by a signal associated with arrival at the cell to be infected (e.g., receptor or co-receptor binding, proton binding in an endosome), they undergo a series of conformational changes. A hydrophobic segment (a “fusion loop” or “fusion peptide”) engages the target-cell membrane and collapse of the bridging intermediate thus formed draws the two membranes (virus and cell) together. We know of three structural classes for viral fusion proteins. Structures for both pre- and postfusion conformations of illustrate the beginning and end points of a process that can be probed by single-virion measurements of fusion kinetics. - Highlights: • Viral fusion proteins overcome the high energy barrier to lipid bilayer merger. • Different molecular structures but the same catalytic mechanism. • Review describes properties of three known fusion-protein structural classes. • Single-virion fusion experiments elucidate mechanism.

Authors:
Publication Date:
OSTI Identifier:
22470171
Resource Type:
Journal Article
Journal Name:
Virology
Additional Journal Information:
Journal Volume: 479-480; Other Information: Copyright (c) 2015 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0042-6822
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; BRIDGES; CATALYSIS; CELL MEMBRANES; CONFORMATIONAL CHANGES; DIFFUSION BARRIERS; LAYERS; LIPIDS; MOLECULAR STRUCTURE; PEPTIDES; PROTONS; RECEPTORS; VIRUSES

Citation Formats

Harrison, Stephen C., E-mail: harrison@crystal.harvard.edu. Viral membrane fusion. United States: N. p., 2015. Web. doi:10.1016/J.VIROL.2015.03.043.
Harrison, Stephen C., E-mail: harrison@crystal.harvard.edu. Viral membrane fusion. United States. doi:10.1016/J.VIROL.2015.03.043.
Harrison, Stephen C., E-mail: harrison@crystal.harvard.edu. Fri . "Viral membrane fusion". United States. doi:10.1016/J.VIROL.2015.03.043.
@article{osti_22470171,
title = {Viral membrane fusion},
author = {Harrison, Stephen C., E-mail: harrison@crystal.harvard.edu},
abstractNote = {Membrane fusion is an essential step when enveloped viruses enter cells. Lipid bilayer fusion requires catalysis to overcome a high kinetic barrier; viral fusion proteins are the agents that fulfill this catalytic function. Despite a variety of molecular architectures, these proteins facilitate fusion by essentially the same generic mechanism. Stimulated by a signal associated with arrival at the cell to be infected (e.g., receptor or co-receptor binding, proton binding in an endosome), they undergo a series of conformational changes. A hydrophobic segment (a “fusion loop” or “fusion peptide”) engages the target-cell membrane and collapse of the bridging intermediate thus formed draws the two membranes (virus and cell) together. We know of three structural classes for viral fusion proteins. Structures for both pre- and postfusion conformations of illustrate the beginning and end points of a process that can be probed by single-virion measurements of fusion kinetics. - Highlights: • Viral fusion proteins overcome the high energy barrier to lipid bilayer merger. • Different molecular structures but the same catalytic mechanism. • Review describes properties of three known fusion-protein structural classes. • Single-virion fusion experiments elucidate mechanism.},
doi = {10.1016/J.VIROL.2015.03.043},
journal = {Virology},
issn = {0042-6822},
number = ,
volume = 479-480,
place = {United States},
year = {2015},
month = {5}
}