Structure, Receptor Binding, and Antigenicity of Influenza Virus Hemagglutinins from the 1957 H2N2 Pandemic▿ †
Identifieur interne : 000078 ( 1968/Analysis ); précédent : 000077; suivant : 000079Structure, Receptor Binding, and Antigenicity of Influenza Virus Hemagglutinins from the 1957 H2N2 Pandemic▿ †
Auteurs : Rui Xu ; Ryan Mcbride ; James C. Paulson ; Christopher F. Basler ; Ian A. WilsonSource :
- Journal of Virology [ 0022-538X ] ; 2009.
Descripteurs français
- KwdFr :
- Animaux, Antigènes viraux (), Antigènes viraux (génétique), Antigènes viraux (histoire), Cristallographie aux rayons X, Données de séquences moléculaires, Flambées de maladies (histoire), Glycoprotéine hémagglutinine du virus influenza (), Glycoprotéine hémagglutinine du virus influenza (génétique), Glycoprotéine hémagglutinine du virus influenza (histoire), Glycoprotéine hémagglutinine du virus influenza (immunologie), Grippe chez les oiseaux (histoire), Grippe chez les oiseaux (virologie), Grippe humaine (histoire), Grippe humaine (virologie), Grippe humaine (épidémiologie), Histoire du 20ème siècle, Humains, Infections à Orthomyxoviridae (histoire), Infections à Orthomyxoviridae (médecine vétérinaire), Infections à Orthomyxoviridae (virologie), Modèles moléculaires, Oiseaux, Récepteurs viraux (physiologie), Similitude de séquences d'acides aminés, Sous-type H2N2 du virus de la grippe A (), Sous-type H2N2 du virus de la grippe A (génétique), Sous-type H2N2 du virus de la grippe A (immunologie), Sous-type H2N2 du virus de la grippe A (pathogénicité), Spécificité d'espèce, Suidae, Séquence d'acides aminés, Zoonoses (histoire), Zoonoses (virologie), Évolution moléculaire.
- MESH :
- génétique : Antigènes viraux, Glycoprotéine hémagglutinine du virus influenza, Sous-type H2N2 du virus de la grippe A.
- histoire : Antigènes viraux, Flambées de maladies, Glycoprotéine hémagglutinine du virus influenza, Grippe chez les oiseaux, Grippe humaine, Infections à Orthomyxoviridae, Zoonoses.
- immunologie : Glycoprotéine hémagglutinine du virus influenza, Sous-type H2N2 du virus de la grippe A.
- médecine vétérinaire : Infections à Orthomyxoviridae.
- pathogénicité : Sous-type H2N2 du virus de la grippe A.
- physiologie : Récepteurs viraux.
- virologie : Grippe chez les oiseaux, Grippe humaine, Infections à Orthomyxoviridae, Zoonoses.
- épidémiologie : Grippe humaine.
- Animaux, Antigènes viraux, Cristallographie aux rayons X, Données de séquences moléculaires, Glycoprotéine hémagglutinine du virus influenza, Histoire du 20ème siècle, Humains, Modèles moléculaires, Oiseaux, Similitude de séquences d'acides aminés, Sous-type H2N2 du virus de la grippe A, Spécificité d'espèce, Suidae, Séquence d'acides aminés, Évolution moléculaire.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antigens, Viral (chemistry), Antigens, Viral (genetics), Antigens, Viral (history), Birds, Crystallography, X-Ray, Disease Outbreaks (history), Evolution, Molecular, Hemagglutinin Glycoproteins, Influenza Virus (chemistry), Hemagglutinin Glycoproteins, Influenza Virus (genetics), Hemagglutinin Glycoproteins, Influenza Virus (history), Hemagglutinin Glycoproteins, Influenza Virus (immunology), History, 20th Century, Humans, Influenza A Virus, H2N2 Subtype (chemistry), Influenza A Virus, H2N2 Subtype (genetics), Influenza A Virus, H2N2 Subtype (immunology), Influenza A Virus, H2N2 Subtype (pathogenicity), Influenza in Birds (history), Influenza in Birds (virology), Influenza, Human (epidemiology), Influenza, Human (history), Influenza, Human (virology), Models, Molecular, Molecular Sequence Data, Orthomyxoviridae Infections (history), Orthomyxoviridae Infections (veterinary), Orthomyxoviridae Infections (virology), Receptors, Virus (physiology), Sequence Homology, Amino Acid, Species Specificity, Swine, Zoonoses (history), Zoonoses (virology).
- MESH :
- chemical , chemistry : Antigens, Viral, Hemagglutinin Glycoproteins, Influenza Virus.
- chemical , genetics : Antigens, Viral, Hemagglutinin Glycoproteins, Influenza Virus.
- chemical , history : Antigens, Viral, Hemagglutinin Glycoproteins, Influenza Virus.
- chemistry : Influenza A Virus, H2N2 Subtype.
- epidemiology : Influenza, Human.
- genetics : Influenza A Virus, H2N2 Subtype.
- history : Disease Outbreaks, Influenza in Birds, Influenza, Human, Orthomyxoviridae Infections, Zoonoses.
- chemical , immunology : Hemagglutinin Glycoproteins, Influenza Virus, Influenza A Virus, H2N2 Subtype.
- pathogenicity : Influenza A Virus, H2N2 Subtype.
- chemical , physiology : Receptors, Virus.
- veterinary : Orthomyxoviridae Infections.
- virology : Influenza in Birds, Influenza, Human, Orthomyxoviridae Infections, Zoonoses.
- Amino Acid Sequence, Animals, Birds, Crystallography, X-Ray, Evolution, Molecular, History, 20th Century, Humans, Models, Molecular, Molecular Sequence Data, Sequence Homology, Amino Acid, Species Specificity, Swine.
Abstract
The hemagglutinin (HA) envelope protein of influenza viruses mediates essential viral functions, including receptor binding and membrane fusion, and is the major viral antigen for antibody neutralization. The 1957 H2N2 subtype (Asian flu) was one of the three great influenza pandemics of the last century and caused 1 million deaths globally from 1957 to 1968. Three crystal structures of 1957 H2 HAs have been determined at 1.60 to 1.75 Å resolutions to investigate the structural basis for their antigenicity and evolution from avian to human binding specificity that contributed to its introduction into the human population. These structures, which represent the highest resolutions yet recorded for a complete ectodomain of a glycosylated viral surface antigen, along with the results of glycan microarray binding analysis, suggest that a hydrophobicity switch at residue 226 and elongation of receptor-binding sites were both critical for avian H2 HA to acquire human receptor specificity. H2 influenza viruses continue to circulate in birds and pigs and, therefore, remain a substantial threat for transmission to humans. The H2 HA structure also reveals a highly conserved epitope that could be harnessed in the design of a broader and more universal influenza A virus vaccine.
Url:
DOI: 10.1128/JVI.02162-09
PubMed: 20007271
PubMed Central: 2812380
Affiliations:
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PMC:2812380Le document en format XML
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Century</term><term>Humans</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Sequence Homology, Amino Acid</term><term>Species Specificity</term><term>Swine</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Antigènes viraux</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Histoire du 20ème siècle</term><term>Humains</term><term>Modèles moléculaires</term><term>Oiseaux</term><term>Similitude de séquences d'acides aminés</term><term>Sous-type H2N2 du virus de la grippe A</term><term>Spécificité d'espèce</term><term>Suidae</term><term>Séquence d'acides aminés</term><term>Évolution moléculaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The hemagglutinin (HA) envelope protein of influenza viruses mediates essential viral functions, including receptor binding and membrane fusion, and is the major viral antigen for antibody neutralization. The 1957 H2N2 subtype (Asian flu) was one of the three great influenza pandemics of the last century and caused 1 million deaths globally from 1957 to 1968. Three crystal structures of 1957 H2 HAs have been determined at 1.60 to 1.75 Å resolutions to investigate the structural basis for their antigenicity and evolution from avian to human binding specificity that contributed to its introduction into the human population. These structures, which represent the highest resolutions yet recorded for a complete ectodomain of a glycosylated viral surface antigen, along with the results of glycan microarray binding analysis, suggest that a hydrophobicity switch at residue 226 and elongation of receptor-binding sites were both critical for avian H2 HA to acquire human receptor specificity. H2 influenza viruses continue to circulate in birds and pigs and, therefore, remain a substantial threat for transmission to humans. The H2 HA structure also reveals a highly conserved epitope that could be harnessed in the design of a broader and more universal influenza A virus vaccine.</p></div></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Basler, Christopher F" sort="Basler, Christopher F" uniqKey="Basler C" first="Christopher F." last="Basler">Christopher F. Basler</name><name sortKey="Mcbride, Ryan" sort="Mcbride, Ryan" uniqKey="Mcbride R" first="Ryan" last="Mcbride">Ryan Mcbride</name><name sortKey="Paulson, James C" sort="Paulson, James C" uniqKey="Paulson J" first="James C." last="Paulson">James C. Paulson</name><name sortKey="Wilson, Ian A" sort="Wilson, Ian A" uniqKey="Wilson I" first="Ian A." last="Wilson">Ian A. Wilson</name><name sortKey="Xu, Rui" sort="Xu, Rui" uniqKey="Xu R" first="Rui" last="Xu">Rui Xu</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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