Entropic forces drive clustering and spatial localization of influenza A M2 during viral budding.
Identifieur interne : 000A05 ( Main/Curation ); 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
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: Pour aller vers cette notice dans l'étape Curation :000248
- to stream PubMed, to step Curation: Pour aller vers cette notice dans l'étape Curation :000248
- to stream PubMed, to step Checkpoint: Pour aller vers cette notice dans l'étape Curation :000277
- to stream Ncbi, to step Merge: Pour aller vers cette notice dans l'étape Curation :000960
- to stream Ncbi, to step Curation: Pour aller vers cette notice dans l'étape Curation :000960
- to stream Ncbi, to step Checkpoint: Pour aller vers cette notice dans l'étape Curation :000960
- to stream Main, to step Merge: Pour aller vers cette notice dans l'étape Curation :000A06
Links to Exploration step
pubmed:30150411Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Entropic forces drive clustering and spatial localization of influenza A M2 during viral budding.</title>
<author><name sortKey="Madsen, Jesper J" sort="Madsen, Jesper J" uniqKey="Madsen J" first="Jesper J" last="Madsen">Jesper J. 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. Voth</name>
<affiliation wicri:level="4"><nlm:affiliation>Department of Chemistry, The University of Chicago, Chicago, IL 60637; gavoth@uchicago.edu.</nlm:affiliation>
<country wicri:rule="url">États-Unis</country>
<wicri:regionArea>Department of Chemistry, The University of Chicago, Chicago</wicri:regionArea>
<placeName><settlement type="city">Chicago</settlement>
<region type="state">Illinois</region>
</placeName>
<orgName type="university">Université de Chicago</orgName>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2018">2018</date>
<idno type="RBID">pubmed:30150411</idno>
<idno type="pmid">30150411</idno>
<idno type="doi">10.1073/pnas.1805443115</idno>
<idno type="wicri:Area/PubMed/Corpus">000248</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000248</idno>
<idno type="wicri:Area/PubMed/Curation">000248</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000248</idno>
<idno type="wicri:Area/PubMed/Checkpoint">000277</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000277</idno>
<idno type="wicri:Area/Ncbi/Merge">000960</idno>
<idno type="wicri:Area/Ncbi/Curation">000960</idno>
<idno type="wicri:Area/Ncbi/Checkpoint">000960</idno>
<idno type="wicri:Area/Main/Merge">000A06</idno>
<idno type="wicri:Area/Main/Curation">000A05</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Entropic forces drive clustering and spatial localization of influenza A M2 during viral budding.</title>
<author><name sortKey="Madsen, Jesper J" sort="Madsen, Jesper J" uniqKey="Madsen J" first="Jesper J" last="Madsen">Jesper J. 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. Voth</name>
<affiliation wicri:level="4"><nlm:affiliation>Department of Chemistry, The University of Chicago, Chicago, IL 60637; gavoth@uchicago.edu.</nlm:affiliation>
<country wicri:rule="url">États-Unis</country>
<wicri:regionArea>Department of Chemistry, The University of Chicago, Chicago</wicri:regionArea>
<placeName><settlement type="city">Chicago</settlement>
<region type="state">Illinois</region>
</placeName>
<orgName type="university">Université de Chicago</orgName>
</affiliation>
</author>
</analytic>
<series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title>
<idno type="eISSN">1091-6490</idno>
<imprint><date when="2018" type="published">2018</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Algorithms</term>
<term>Animals</term>
<term>Cell Membrane (chemistry)</term>
<term>Cell Membrane (ultrastructure)</term>
<term>Cell Membrane (virology)</term>
<term>Dogs</term>
<term>Entropy</term>
<term>Host-Pathogen Interactions</term>
<term>Madin Darby Canine Kidney Cells</term>
<term>Membrane Lipids (chemistry)</term>
<term>Microscopy, Electron</term>
<term>Models, Biological</term>
<term>Molecular Dynamics Simulation</term>
<term>Viral Matrix Proteins (physiology)</term>
<term>Virus Assembly</term>
<term>Virus Release</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Algorithmes</term>
<term>Animaux</term>
<term>Assemblage viral</term>
<term>Cellules rénales canines Madin-Darby</term>
<term>Chiens</term>
<term>Entropie</term>
<term>Interactions hôte-pathogène</term>
<term>Libération de particules virales</term>
<term>Lipides membranaires ()</term>
<term>Membrane cellulaire ()</term>
<term>Membrane cellulaire (ultrastructure)</term>
<term>Membrane cellulaire (virologie)</term>
<term>Microscopie électronique</term>
<term>Modèles biologiques</term>
<term>Protéines de la matrice virale (physiologie)</term>
<term>Simulation de dynamique moléculaire</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Lipids</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Cell Membrane</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Protéines de la matrice virale</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Viral Matrix Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Cell Membrane</term>
</keywords>
<keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Membrane cellulaire</term>
</keywords>
<keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Cell Membrane</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Algorithms</term>
<term>Animals</term>
<term>Dogs</term>
<term>Entropy</term>
<term>Host-Pathogen Interactions</term>
<term>Madin Darby Canine Kidney Cells</term>
<term>Microscopy, Electron</term>
<term>Models, Biological</term>
<term>Molecular Dynamics Simulation</term>
<term>Virus Assembly</term>
<term>Virus Release</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Algorithmes</term>
<term>Animaux</term>
<term>Assemblage viral</term>
<term>Cellules rénales canines Madin-Darby</term>
<term>Chiens</term>
<term>Entropie</term>
<term>Interactions hôte-pathogène</term>
<term>Libération de particules virales</term>
<term>Lipides membranaires</term>
<term>Membrane cellulaire</term>
<term>Microscopie électronique</term>
<term>Modèles biologiques</term>
<term>Simulation de dynamique moléculaire</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">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.</div>
</front>
</TEI>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/StressCovidV1/Data/Main/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000A05 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Curation/biblio.hfd -nk 000A05 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= StressCovidV1 |flux= Main |étape= Curation |type= RBID |clé= pubmed:30150411 |texte= Entropic forces drive clustering and spatial localization of influenza A M2 during viral budding. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Curation/RBID.i -Sk "pubmed:30150411" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Curation/biblio.hfd \ | NlmPubMed2Wicri -a StressCovidV1
This area was generated with Dilib version V0.6.33. |