Entropic forces drive clustering and spatial localization of influenza A M2 during viral budding.
Identifieur interne : 000A05 ( Main/Exploration ); précédent : 000A04; suivant : 000A06Entropic forces drive clustering and spatial localization of influenza A M2 during viral budding.
Auteurs : Jesper J. Madsen [États-Unis] ; John M A. Grime [États-Unis] ; Jeremy S. Rossman [Royaume-Uni] ; Gregory A. Voth [États-Unis]Source :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2018.
Descripteurs français
- KwdFr :
- Algorithmes, Animaux, Assemblage viral, Cellules rénales canines Madin-Darby, Chiens, Entropie, Interactions hôte-pathogène, Libération de particules virales, Lipides membranaires (), Membrane cellulaire (), Membrane cellulaire (ultrastructure), Membrane cellulaire (virologie), Microscopie électronique, Modèles biologiques, Protéines de la matrice virale (physiologie), Simulation de dynamique moléculaire.
- MESH :
- physiologie : Protéines de la matrice virale.
- virologie : Membrane cellulaire.
- Algorithmes, Animaux, Assemblage viral, Cellules rénales canines Madin-Darby, Chiens, Entropie, Interactions hôte-pathogène, Libération de particules virales, Lipides membranaires, Membrane cellulaire, Microscopie électronique, Modèles biologiques, Simulation de dynamique moléculaire.
English descriptors
- KwdEn :
- Algorithms, Animals, Cell Membrane (chemistry), Cell Membrane (ultrastructure), Cell Membrane (virology), Dogs, Entropy, Host-Pathogen Interactions, Madin Darby Canine Kidney Cells, Membrane Lipids (chemistry), Microscopy, Electron, Models, Biological, Molecular Dynamics Simulation, Viral Matrix Proteins (physiology), Virus Assembly, Virus Release.
- MESH :
- chemical , chemistry : Membrane Lipids.
- chemistry : Cell Membrane.
- chemical , physiology : Viral Matrix Proteins.
- ultrastructure : Cell Membrane.
- virology : Cell Membrane.
- Algorithms, Animals, Dogs, Entropy, Host-Pathogen Interactions, Madin Darby Canine Kidney Cells, Microscopy, Electron, Models, Biological, Molecular Dynamics Simulation, Virus Assembly, Virus Release.
Abstract
The influenza A matrix 2 (M2) transmembrane protein facilitates virion release from the infected host cell. In particular, M2 plays a role in the induction of membrane curvature and/or in the scission process whereby the envelope is cut upon virion release. Here we show using coarse-grained computer simulations that various M2 assembly geometries emerge due to an entropic driving force, resulting in compact clusters or linearly extended aggregates as a direct consequence of the lateral membrane stresses. Conditions under which these protein assemblies will cause the lipid membrane to curve are explored, and we predict that a critical cluster size is required for this to happen. We go on to demonstrate that under the stress conditions taking place in the cellular membrane as it undergoes large-scale membrane remodeling, the M2 protein will, in principle, be able to both contribute to curvature induction and sense curvature to line up in manifolds where local membrane line tension is high. M2 is found to exhibit linactant behavior in liquid-disordered-liquid-ordered phase-separated lipid mixtures and to be excluded from the liquid-ordered phase, in near-quantitative agreement with experimental observations. Our findings support a role for M2 in membrane remodeling during influenza viral budding both as an inducer and a sensor of membrane curvature, and they suggest a mechanism by which localization of M2 can occur as the virion assembles and releases from the host cell, independent of how the membrane curvature is produced.
DOI: 10.1073/pnas.1805443115
PubMed: 30150411
Affiliations:
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Le document en format XML
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Madsen</name><affiliation wicri:level="2"><nlm:affiliation>Department of Chemistry, The University of Chicago, Chicago, IL 60637.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Illinois</region></placeName><wicri:cityArea>Department of Chemistry, The University of Chicago, Chicago</wicri:cityArea></affiliation></author><author><name sortKey="Grime, John M A" sort="Grime, John M A" uniqKey="Grime J" first="John M A" last="Grime">John M A. Grime</name><affiliation wicri:level="2"><nlm:affiliation>Department of Chemistry, The University of Chicago, Chicago, IL 60637.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Illinois</region></placeName><wicri:cityArea>Department of Chemistry, The University of Chicago, Chicago</wicri:cityArea></affiliation></author><author><name sortKey="Rossman, Jeremy S" sort="Rossman, Jeremy S" uniqKey="Rossman J" first="Jeremy S" last="Rossman">Jeremy S. Rossman</name><affiliation wicri:level="1"><nlm:affiliation>School of Biosciences, University of Kent, Canterbury, CT2 7NJ Kent, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>School of Biosciences, University of Kent, Canterbury, CT2 7NJ Kent</wicri:regionArea><wicri:noRegion>CT2 7NJ Kent</wicri:noRegion></affiliation></author><author><name sortKey="Voth, Gregory A" sort="Voth, Gregory A" uniqKey="Voth G" first="Gregory A" last="Voth">Gregory A. 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In particular, M2 plays a role in the induction of membrane curvature and/or in the scission process whereby the envelope is cut upon virion release. Here we show using coarse-grained computer simulations that various M2 assembly geometries emerge due to an entropic driving force, resulting in compact clusters or linearly extended aggregates as a direct consequence of the lateral membrane stresses. Conditions under which these protein assemblies will cause the lipid membrane to curve are explored, and we predict that a critical cluster size is required for this to happen. We go on to demonstrate that under the stress conditions taking place in the cellular membrane as it undergoes large-scale membrane remodeling, the M2 protein will, in principle, be able to both contribute to curvature induction and sense curvature to line up in manifolds where local membrane line tension is high. M2 is found to exhibit linactant behavior in liquid-disordered-liquid-ordered phase-separated lipid mixtures and to be excluded from the liquid-ordered phase, in near-quantitative agreement with experimental observations. Our findings support a role for M2 in membrane remodeling during influenza viral budding both as an inducer and a sensor of membrane curvature, and they suggest a mechanism by which localization of M2 can occur as the virion assembles and releases from the host cell, independent of how the membrane curvature is produced.</div></front></TEI><affiliations><list><country><li>Royaume-Uni</li><li>États-Unis</li></country><region><li>Illinois</li></region><settlement><li>Chicago</li></settlement><orgName><li>Université de Chicago</li></orgName></list><tree><country name="États-Unis"><region name="Illinois"><name sortKey="Madsen, Jesper J" sort="Madsen, Jesper J" uniqKey="Madsen J" first="Jesper J" last="Madsen">Jesper J. Madsen</name></region><name sortKey="Grime, John M A" sort="Grime, John M A" uniqKey="Grime J" first="John M A" last="Grime">John M A. Grime</name><name sortKey="Voth, Gregory A" sort="Voth, Gregory A" uniqKey="Voth G" first="Gregory A" last="Voth">Gregory A. Voth</name></country><country name="Royaume-Uni"><noRegion><name sortKey="Rossman, Jeremy S" sort="Rossman, Jeremy S" uniqKey="Rossman J" first="Jeremy S" last="Rossman">Jeremy S. Rossman</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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