Analysis of Adaptation Mutants in the Hemagglutinin of the Influenza A(H1N1)pdm09 Virus
Identifieur interne : 001401 ( Main/Exploration ); précédent : 001400; suivant : 001402Analysis of Adaptation Mutants in the Hemagglutinin of the Influenza A(H1N1)pdm09 Virus
Auteurs : Alicia Jiménez-Alberto [Mexique] ; Esmeralda Alvarado-Facundo [Mexique, États-Unis] ; Rosa María Ribas-Aparicio [Mexique] ; Juan A. Castelán-Vega [Mexique]Source :
- PLoS ONE [ 1932-6203 ] ; 2013.
Descripteurs français
- KwdFr :
- Adaptation physiologique (génétique), Glycoprotéine hémagglutinine du virus influenza (), Glycoprotéine hémagglutinine du virus influenza (génétique), Glycoprotéine hémagglutinine du virus influenza (immunologie), Glycoprotéine hémagglutinine du virus influenza (métabolisme), Grippe humaine (virologie), Grippe humaine (épidémiologie), Humains, Pandémie de grippe de 1918-1919, Propriétés de surface, Simulation de dynamique moléculaire, Sous-type H1N1 du virus de la grippe A (génétique), Sous-type H1N1 du virus de la grippe A (immunologie), Sous-type H1N1 du virus de la grippe A (métabolisme), Sous-type H1N1 du virus de la grippe A (physiologie), Thermodynamique, Électricité statique, Épidémiologie moléculaire.
- MESH :
- génétique : Adaptation physiologique, Glycoprotéine hémagglutinine du virus influenza, Sous-type H1N1 du virus de la grippe A.
- immunologie : Glycoprotéine hémagglutinine du virus influenza, Sous-type H1N1 du virus de la grippe A.
- métabolisme : Glycoprotéine hémagglutinine du virus influenza, Sous-type H1N1 du virus de la grippe A.
- physiologie : Sous-type H1N1 du virus de la grippe A.
- virologie : Grippe humaine.
- épidémiologie : Grippe humaine.
- Glycoprotéine hémagglutinine du virus influenza, Humains, Pandémie de grippe de 1918-1919, Propriétés de surface, Simulation de dynamique moléculaire, Thermodynamique, Électricité statique, Épidémiologie moléculaire.
English descriptors
- KwdEn :
- Adaptation, Physiological (genetics), Hemagglutinin Glycoproteins, Influenza Virus (chemistry), Hemagglutinin Glycoproteins, Influenza Virus (genetics), Hemagglutinin Glycoproteins, Influenza Virus (immunology), Hemagglutinin Glycoproteins, Influenza Virus (metabolism), Humans, Influenza A Virus, H1N1 Subtype (genetics), Influenza A Virus, H1N1 Subtype (immunology), Influenza A Virus, H1N1 Subtype (metabolism), Influenza A Virus, H1N1 Subtype (physiology), Influenza Pandemic, 1918-1919, Influenza, Human (epidemiology), Influenza, Human (virology), Molecular Dynamics Simulation, Molecular Epidemiology, Static Electricity, Surface Properties, Thermodynamics.
- MESH :
- chemical , chemistry : Hemagglutinin Glycoproteins, Influenza Virus.
- epidemiology : Influenza, Human.
- genetics : Adaptation, Physiological, Hemagglutinin Glycoproteins, Influenza Virus, Influenza A Virus, H1N1 Subtype.
- chemical , immunology : Hemagglutinin Glycoproteins, Influenza Virus, Influenza A Virus, H1N1 Subtype.
- chemical , metabolism : Hemagglutinin Glycoproteins, Influenza Virus, Influenza A Virus, H1N1 Subtype.
- physiology : Influenza A Virus, H1N1 Subtype.
- virology : Influenza, Human.
- Humans, Influenza Pandemic, 1918-1919, Molecular Dynamics Simulation, Molecular Epidemiology, Static Electricity, Surface Properties, Thermodynamics.
Abstract
Hemagglutinin is the major surface glycoprotein of influenza viruses. It participates in the initial steps of viral infection through receptor binding and membrane fusion events. The influenza pandemic of 2009 provided a unique scenario to study virus evolution. We performed molecular dynamics simulations with four hemagglutinin variants that appeared throughout the 2009 influenza A (H1N1) pandemic. We found that variant 1 (S143G, S185T) likely arose to avoid immune recognition. Variant 2 (A134T), and variant 3 (D222E, P297S) had an increased binding affinity for the receptor. Finally, variant 4 (E374K) altered hemagglutinin stability in the vicinity of the fusion peptide. Variants 1 and 4 have become increasingly predominant, while variants 2 and 3 declined as the pandemic progressed. Our results show some of the different strategies that the influenza virus uses to adapt to the human host and provide an example of how selective pressure drives antigenic drift in viral proteins.
Url:
DOI: 10.1371/journal.pone.0070005
PubMed: 23894575
PubMed Central: 3720954
Affiliations:
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Le document en format XML
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Virus (immunology)</term><term>Hemagglutinin Glycoproteins, Influenza Virus (metabolism)</term><term>Humans</term><term>Influenza A Virus, H1N1 Subtype (genetics)</term><term>Influenza A Virus, H1N1 Subtype (immunology)</term><term>Influenza A Virus, H1N1 Subtype (metabolism)</term><term>Influenza A Virus, H1N1 Subtype (physiology)</term><term>Influenza Pandemic, 1918-1919</term><term>Influenza, Human (epidemiology)</term><term>Influenza, Human (virology)</term><term>Molecular Dynamics Simulation</term><term>Molecular Epidemiology</term><term>Static Electricity</term><term>Surface Properties</term><term>Thermodynamics</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Adaptation physiologique (génétique)</term><term>Glycoprotéine hémagglutinine du virus influenza ()</term><term>Glycoprotéine hémagglutinine du virus influenza (génétique)</term><term>Glycoprotéine hémagglutinine du virus influenza (immunologie)</term><term>Glycoprotéine hémagglutinine du virus influenza (métabolisme)</term><term>Grippe humaine (virologie)</term><term>Grippe humaine (épidémiologie)</term><term>Humains</term><term>Pandémie de grippe de 1918-1919</term><term>Propriétés de surface</term><term>Simulation de dynamique moléculaire</term><term>Sous-type H1N1 du virus de la grippe A (génétique)</term><term>Sous-type H1N1 du virus de la grippe A (immunologie)</term><term>Sous-type H1N1 du virus de la grippe A (métabolisme)</term><term>Sous-type H1N1 du virus de la grippe A (physiologie)</term><term>Thermodynamique</term><term>Électricité statique</term><term>Épidémiologie moléculaire</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Hemagglutinin Glycoproteins, Influenza Virus</term></keywords><keywords scheme="MESH" qualifier="epidemiology" xml:lang="en"><term>Influenza, Human</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Adaptation, Physiological</term><term>Hemagglutinin Glycoproteins, Influenza Virus</term><term>Influenza A Virus, H1N1 Subtype</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Adaptation physiologique</term><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Sous-type H1N1 du virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Sous-type H1N1 du virus de la grippe A</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Hemagglutinin Glycoproteins, Influenza Virus</term><term>Influenza A Virus, H1N1 Subtype</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Hemagglutinin Glycoproteins, Influenza Virus</term><term>Influenza A Virus, H1N1 Subtype</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Sous-type H1N1 du virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Sous-type H1N1 du virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Influenza A Virus, H1N1 Subtype</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Grippe humaine</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Influenza, Human</term></keywords><keywords scheme="MESH" qualifier="épidémiologie" xml:lang="fr"><term>Grippe humaine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Influenza Pandemic, 1918-1919</term><term>Molecular Dynamics Simulation</term><term>Molecular Epidemiology</term><term>Static Electricity</term><term>Surface Properties</term><term>Thermodynamics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Humains</term><term>Pandémie de grippe de 1918-1919</term><term>Propriétés de surface</term><term>Simulation de dynamique moléculaire</term><term>Thermodynamique</term><term>Électricité statique</term><term>Épidémiologie moléculaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Hemagglutinin is the major surface glycoprotein of influenza viruses. It participates in the initial steps of viral infection through receptor binding and membrane fusion events. The influenza pandemic of 2009 provided a unique scenario to study virus evolution. We performed molecular dynamics simulations with four hemagglutinin variants that appeared throughout the 2009 influenza A (H1N1) pandemic. We found that variant 1 (S143G, S185T) likely arose to avoid immune recognition. Variant 2 (A134T), and variant 3 (D222E, P297S) had an increased binding affinity for the receptor. Finally, variant 4 (E374K) altered hemagglutinin stability in the vicinity of the fusion peptide. Variants 1 and 4 have become increasingly predominant, while variants 2 and 3 declined as the pandemic progressed. Our results show some of the different strategies that the influenza virus uses to adapt to the human host and provide an example of how selective pressure drives antigenic drift in viral proteins.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Varki, Nm" uniqKey="Varki N">NM Varki</name></author><author><name sortKey="Varki, A" uniqKey="Varki A">A Varki</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Skehel, Jj" uniqKey="Skehel J">JJ Skehel</name></author><author><name sortKey="Wiley, Dc" uniqKey="Wiley D">DC Wiley</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Bouvier, Nm" uniqKey="Bouvier N">NM Bouvier</name></author><author><name sortKey="Palese, P" uniqKey="Palese P">P Palese</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Chutinimitkul, S" uniqKey="Chutinimitkul S">S Chutinimitkul</name></author><author><name sortKey="Herfst, S" uniqKey="Herfst S">S Herfst</name></author><author><name sortKey="Steel, J" uniqKey="Steel J">J Steel</name></author><author><name sortKey="Lowen, Ac" uniqKey="Lowen A">AC Lowen</name></author><author><name sortKey="Ye, J" uniqKey="Ye J">J Ye</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Belser, Ja" uniqKey="Belser J">JA Belser</name></author><author><name sortKey="Jayaraman, A" uniqKey="Jayaraman A">A Jayaraman</name></author><author><name sortKey="Raman, R" uniqKey="Raman R">R Raman</name></author><author><name sortKey="Pappas, C" uniqKey="Pappas C">C Pappas</name></author><author><name sortKey="Zeng, H" uniqKey="Zeng H">H Zeng</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Rykkvin, R" uniqKey="Rykkvin R">R Rykkvin</name></author><author><name sortKey="Kilander, A" uniqKey="Kilander A">A Kilander</name></author><author><name sortKey="Dudman, Sg" uniqKey="Dudman S">SG 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sort="Alvarado Facundo, Esmeralda" uniqKey="Alvarado Facundo E" first="Esmeralda" last="Alvarado-Facundo">Esmeralda Alvarado-Facundo</name><name sortKey="Castelan Vega, Juan A" sort="Castelan Vega, Juan A" uniqKey="Castelan Vega J" first="Juan A." last="Castelán-Vega">Juan A. Castelán-Vega</name><name sortKey="Ribas Aparicio, Rosa Maria" sort="Ribas Aparicio, Rosa Maria" uniqKey="Ribas Aparicio R" first="Rosa María" last="Ribas-Aparicio">Rosa María Ribas-Aparicio</name></country><country name="États-Unis"><region name="Maryland"><name sortKey="Alvarado Facundo, Esmeralda" sort="Alvarado Facundo, Esmeralda" uniqKey="Alvarado Facundo E" first="Esmeralda" last="Alvarado-Facundo">Esmeralda Alvarado-Facundo</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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