Structural Analysis of the Hemagglutinin from the Recent 2013 H7N9 Influenza Virus
Identifieur interne : 000829 ( Main/Exploration ); précédent : 000828; suivant : 000830Structural Analysis of the Hemagglutinin from the Recent 2013 H7N9 Influenza Virus
Auteurs : Hua Yang ; Paul J. Carney ; Jessie C. Chang ; Julie M. Villanueva ; James StevensSource :
- Journal of Virology [ 0022-538X ] ; 2013.
Descripteurs français
- KwdFr :
- Conformation des protéines, Cristallisation, Cristallographie aux rayons X, Données de séquences moléculaires, Glycoprotéine hémagglutinine du virus influenza (), Glycoprotéine hémagglutinine du virus influenza (génétique), Glycoprotéine hémagglutinine du virus influenza (métabolisme), Grippe humaine (génétique), Grippe humaine (métabolisme), Grippe humaine (virologie), Humains, Liaison aux protéines, Mutation (génétique), Polyosides (métabolisme), Protéines recombinantes (génétique), Protéines recombinantes (isolement et purification), Protéines recombinantes (métabolisme), Similitude de séquences d'acides aminés, Sites de fixation, Sous-type H7N9 du virus de la grippe A (physiologie), Substitution d'acide aminé, Séquence d'acides aminés.
- MESH :
- génétique : Glycoprotéine hémagglutinine du virus influenza, Grippe humaine, Mutation, Protéines recombinantes.
- isolement et purification : Protéines recombinantes.
- métabolisme : Glycoprotéine hémagglutinine du virus influenza, Grippe humaine, Polyosides, Protéines recombinantes.
- physiologie : Sous-type H7N9 du virus de la grippe A.
- virologie : Grippe humaine.
- Conformation des protéines, Cristallisation, Cristallographie aux rayons X, Données de séquences moléculaires, Glycoprotéine hémagglutinine du virus influenza, Humains, Liaison aux protéines, Similitude de séquences d'acides aminés, Sites de fixation, Substitution d'acide aminé, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Amino Acid Substitution, Binding Sites, Crystallization, Crystallography, X-Ray, Hemagglutinin Glycoproteins, Influenza Virus (chemistry), Hemagglutinin Glycoproteins, Influenza Virus (genetics), Hemagglutinin Glycoproteins, Influenza Virus (metabolism), Humans, Influenza A Virus, H7N9 Subtype (physiology), Influenza, Human (genetics), Influenza, Human (metabolism), Influenza, Human (virology), Molecular Sequence Data, Mutation (genetics), Polysaccharides (metabolism), Protein Binding, Protein Conformation, Recombinant Proteins (genetics), Recombinant Proteins (isolation & purification), Recombinant Proteins (metabolism), Sequence Homology, Amino Acid.
- MESH :
- chemical , chemistry : Hemagglutinin Glycoproteins, Influenza Virus.
- chemical , genetics : Hemagglutinin Glycoproteins, Influenza Virus, Recombinant Proteins.
- chemical , isolation & purification : Recombinant Proteins.
- chemical , metabolism : Hemagglutinin Glycoproteins, Influenza Virus, Polysaccharides, Recombinant Proteins.
- genetics : Influenza, Human, Mutation.
- metabolism : Influenza, Human.
- physiology : Influenza A Virus, H7N9 Subtype.
- virology : Influenza, Human.
- Amino Acid Sequence, Amino Acid Substitution, Binding Sites, Crystallization, Crystallography, X-Ray, Humans, Molecular Sequence Data, Protein Binding, Protein Conformation, Sequence Homology, Amino Acid.
Abstract
In March 2013, the Chinese Center for Disease Control and Prevention reported human infections with an H7N9 influenza virus, and by 20 July 2013, the numbers of laboratory-confirmed cases had climbed to 134, including 43 fatalities and 127 hospitalizations. The newly emerging H7N9 viruses constitute an obvious public health concern because of the apparent severity of this outbreak. Here we focus on the hemagglutinins (HAs) of these viruses and assess their receptor binding phenotype in relation to previous HAs studied. Glycan microarray and kinetic analyses of recombinant A(H7N9) HAs were performed to compare the receptor binding profile of wild-type receptor binding site variants at position 217, a residue analogous to one of two positions known to switch avian to human receptor preference in H2N2 and H3N2 viruses. Two recombinant A(H7N9) HAs were structurally characterized, and a mutational study of the receptor binding site was performed to analyze important residues that can affect receptor preference and affinity. Results highlight a weak human receptor preference of the H7N9 HAs, suggesting that these viruses require further adaptation in order to adapt fully to humans.
Url:
DOI: 10.1128/JVI.01854-13
PubMed: 24027325
PubMed Central: 3807915
Affiliations:
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Le document en format XML
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(virology)</term><term>Molecular Sequence Data</term><term>Mutation (genetics)</term><term>Polysaccharides (metabolism)</term><term>Protein Binding</term><term>Protein Conformation</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (isolation & purification)</term><term>Recombinant Proteins (metabolism)</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines</term><term>Cristallisation</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Glycoprotéine hémagglutinine du virus influenza ()</term><term>Glycoprotéine hémagglutinine du virus influenza (génétique)</term><term>Glycoprotéine hémagglutinine du virus influenza (métabolisme)</term><term>Grippe humaine (génétique)</term><term>Grippe humaine (métabolisme)</term><term>Grippe humaine (virologie)</term><term>Humains</term><term>Liaison aux protéines</term><term>Mutation 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influenza</term><term>Humains</term><term>Liaison aux protéines</term><term>Similitude de séquences d'acides aminés</term><term>Sites de fixation</term><term>Substitution d'acide aminé</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>In March 2013, the Chinese Center for Disease Control and Prevention reported human infections with an H7N9 influenza virus, and by 20 July 2013, the numbers of laboratory-confirmed cases had climbed to 134, including 43 fatalities and 127 hospitalizations. The newly emerging H7N9 viruses constitute an obvious public health concern because of the apparent severity of this outbreak. Here we focus on the hemagglutinins (HAs) of these viruses and assess their receptor binding phenotype in relation to previous HAs studied. Glycan microarray and kinetic analyses of recombinant A(H7N9) HAs were performed to compare the receptor binding profile of wild-type receptor binding site variants at position 217, a residue analogous to one of two positions known to switch avian to human receptor preference in H2N2 and H3N2 viruses. Two recombinant A(H7N9) HAs were structurally characterized, and a mutational study of the receptor binding site was performed to analyze important residues that can affect receptor preference and affinity. Results highlight a weak human receptor preference of the H7N9 HAs, suggesting that these viruses require further adaptation in order to adapt fully to humans.</p></div></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Carney, Paul J" sort="Carney, Paul J" uniqKey="Carney P" first="Paul J." last="Carney">Paul J. Carney</name><name sortKey="Chang, Jessie C" sort="Chang, Jessie C" uniqKey="Chang J" first="Jessie C." last="Chang">Jessie C. Chang</name><name sortKey="Stevens, James" sort="Stevens, James" uniqKey="Stevens J" first="James" last="Stevens">James Stevens</name><name sortKey="Villanueva, Julie M" sort="Villanueva, Julie M" uniqKey="Villanueva J" first="Julie M." last="Villanueva">Julie M. Villanueva</name><name sortKey="Yang, Hua" sort="Yang, Hua" uniqKey="Yang H" first="Hua" last="Yang">Hua Yang</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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