Preferential recognition of avian-like receptors in human influenza A H7N9 viruses
Identifieur interne : 000849 ( Main/Exploration ); précédent : 000848; suivant : 000850Preferential recognition of avian-like receptors in human influenza A H7N9 viruses
Auteurs : Rui Xu [États-Unis] ; Robert P. De Vries [États-Unis] ; Xueyong Zhu [États-Unis] ; Corwin M. Nycholat [États-Unis] ; Ryan Mcbride [États-Unis] ; Wenli Yu [États-Unis] ; James C. Paulson [États-Unis] ; Ian A. Wilson [États-Unis]Source :
- Science (New York, N.Y.) [ 0036-8075 ] ; 2013.
Descripteurs français
- KwdFr :
- Analyse sur microréseau, Animaux, Conformation des glucides, Cristallographie aux rayons X, Données de séquences moléculaires, Glycoprotéine hémagglutinine du virus influenza (), Glycoprotéine hémagglutinine du virus influenza (métabolisme), Grippe chez les oiseaux (transmission), Grippe chez les oiseaux (virologie), Grippe humaine (transmission), Grippe humaine (virologie), Humains, Ligands, Modèles moléculaires, Mutation, Oiseaux, Polyosides (), Polyosides (métabolisme), Protéines recombinantes (), Protéines recombinantes (métabolisme), Récepteurs viraux (), Récepteurs viraux (métabolisme), Sites de fixation, Sous-type H7N9 du virus de la grippe A (métabolisme), Sous-type H7N9 du virus de la grippe A (pathogénicité), Séquence d'acides aminés.
- MESH :
- métabolisme : Glycoprotéine hémagglutinine du virus influenza, Polyosides, Protéines recombinantes, Récepteurs viraux, Sous-type H7N9 du virus de la grippe A.
- pathogénicité : Sous-type H7N9 du virus de la grippe A.
- virologie : Grippe chez les oiseaux, Grippe humaine.
- Analyse sur microréseau, Animaux, Conformation des glucides, Cristallographie aux rayons X, Données de séquences moléculaires, Glycoprotéine hémagglutinine du virus influenza, Grippe chez les oiseaux, Grippe humaine, Humains, Ligands, Modèles moléculaires, Mutation, Oiseaux, Polyosides, Protéines recombinantes, Récepteurs viraux, Sites de fixation, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Binding Sites, Birds, Carbohydrate Conformation, Crystallography, X-Ray, Hemagglutinin Glycoproteins, Influenza Virus (chemistry), Hemagglutinin Glycoproteins, Influenza Virus (metabolism), Humans, Influenza A Virus, H7N9 Subtype (metabolism), Influenza A Virus, H7N9 Subtype (pathogenicity), Influenza in Birds (transmission), Influenza in Birds (virology), Influenza, Human (transmission), Influenza, Human (virology), Ligands, Microarray Analysis, Models, Molecular, Molecular Sequence Data, Mutation, Polysaccharides (chemistry), Polysaccharides (metabolism), Receptors, Virus (chemistry), Receptors, Virus (metabolism), Recombinant Proteins (chemistry), Recombinant Proteins (metabolism).
- MESH :
- chemical , chemistry : Hemagglutinin Glycoproteins, Influenza Virus, Polysaccharides, Receptors, Virus, Recombinant Proteins.
- chemical , metabolism : Hemagglutinin Glycoproteins, Influenza Virus, Polysaccharides, Receptors, Virus, Recombinant Proteins.
- metabolism : Influenza A Virus, H7N9 Subtype.
- pathogenicity : Influenza A Virus, H7N9 Subtype.
- transmission : Influenza in Birds, Influenza, Human.
- virology : Influenza in Birds, Influenza, Human.
- Amino Acid Sequence, Animals, Binding Sites, Birds, Carbohydrate Conformation, Crystallography, X-Ray, Humans, Ligands, Microarray Analysis, Models, Molecular, Molecular Sequence Data, Mutation.
Abstract
The 2013 outbreak of avian-origin H7N9 influenza in eastern China has raised concerns about its ability to transmit in the human population. The hemagglutinin glycoprotein of most human H7N9 viruses carries Leu226, a residue linked to adaptation of H2N2 and H3N2 pandemic viruses to human receptors. However, glycan array analysis of the H7 hemagglutinin reveals negligible binding to human-like α2-6-linked receptors and strong preference for a subset of avian-like α2-3-linked glycans recognized by all avian H7 viruses. Crystal structures of H7N9 hemagglutinin and six hemagglutinin-glycan complexes have elucidated the structural basis for preferential recognition of avian-like receptors. These findings suggest that the current human H7N9 viruses are poorly adapted for efficient human-to-human transmission.
Url:
DOI: 10.1126/science.1243761
PubMed: 24311689
PubMed Central: 3954636
Affiliations:
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De Vries</name><affiliation wicri:level="2"><nlm:aff id="A2">Department of Cell and Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Cell and Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation><affiliation wicri:level="2"><nlm:aff id="A3">Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author><author><name sortKey="Zhu, Xueyong" sort="Zhu, Xueyong" uniqKey="Zhu X" first="Xueyong" last="Zhu">Xueyong Zhu</name><affiliation wicri:level="2"><nlm:aff id="A1">Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author><author><name sortKey="Nycholat, Corwin M" sort="Nycholat, Corwin M" uniqKey="Nycholat C" first="Corwin M." last="Nycholat">Corwin M. Nycholat</name><affiliation wicri:level="2"><nlm:aff id="A2">Department of Cell and Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Cell and Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation><affiliation wicri:level="2"><nlm:aff id="A3">Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author><author><name sortKey="Mcbride, Ryan" sort="Mcbride, Ryan" uniqKey="Mcbride R" first="Ryan" last="Mcbride">Ryan Mcbride</name><affiliation wicri:level="2"><nlm:aff id="A2">Department of Cell and Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Cell and Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation><affiliation wicri:level="2"><nlm:aff id="A3">Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author><author><name sortKey="Yu, Wenli" sort="Yu, Wenli" uniqKey="Yu W" first="Wenli" last="Yu">Wenli Yu</name><affiliation wicri:level="2"><nlm:aff id="A1">Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author><author><name sortKey="Paulson, James C" sort="Paulson, James C" uniqKey="Paulson J" first="James C." last="Paulson">James C. Paulson</name><affiliation wicri:level="2"><nlm:aff id="A2">Department of Cell and Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Cell and Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation><affiliation wicri:level="2"><nlm:aff id="A3">Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author><author><name sortKey="Wilson, Ian A" sort="Wilson, Ian A" uniqKey="Wilson I" first="Ian A." last="Wilson">Ian A. Wilson</name><affiliation wicri:level="2"><nlm:aff id="A1">Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation><affiliation wicri:level="2"><nlm:aff id="A4">Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author></analytic><series><title level="j">Science (New York, N.Y.)</title><idno type="ISSN">0036-8075</idno><idno type="eISSN">1095-9203</idno><imprint><date when="2013">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Binding Sites</term><term>Birds</term><term>Carbohydrate Conformation</term><term>Crystallography, X-Ray</term><term>Hemagglutinin Glycoproteins, Influenza Virus (chemistry)</term><term>Hemagglutinin Glycoproteins, Influenza Virus (metabolism)</term><term>Humans</term><term>Influenza A Virus, H7N9 Subtype (metabolism)</term><term>Influenza A Virus, H7N9 Subtype (pathogenicity)</term><term>Influenza in Birds (transmission)</term><term>Influenza in Birds (virology)</term><term>Influenza, Human (transmission)</term><term>Influenza, Human (virology)</term><term>Ligands</term><term>Microarray Analysis</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Mutation</term><term>Polysaccharides (chemistry)</term><term>Polysaccharides (metabolism)</term><term>Receptors, Virus (chemistry)</term><term>Receptors, Virus (metabolism)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Analyse sur microréseau</term><term>Animaux</term><term>Conformation des glucides</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 (métabolisme)</term><term>Grippe chez les oiseaux (transmission)</term><term>Grippe chez les oiseaux (virologie)</term><term>Grippe humaine (transmission)</term><term>Grippe humaine (virologie)</term><term>Humains</term><term>Ligands</term><term>Modèles moléculaires</term><term>Mutation</term><term>Oiseaux</term><term>Polyosides ()</term><term>Polyosides (métabolisme)</term><term>Protéines recombinantes ()</term><term>Protéines recombinantes (métabolisme)</term><term>Récepteurs viraux ()</term><term>Récepteurs viraux (métabolisme)</term><term>Sites de fixation</term><term>Sous-type H7N9 du virus de la grippe A (métabolisme)</term><term>Sous-type H7N9 du virus de la grippe A (pathogénicité)</term><term>Séquence d'acides aminés</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Hemagglutinin Glycoproteins, Influenza Virus</term><term>Polysaccharides</term><term>Receptors, Virus</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Hemagglutinin Glycoproteins, Influenza Virus</term><term>Polysaccharides</term><term>Receptors, Virus</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Influenza A Virus, H7N9 Subtype</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Polyosides</term><term>Protéines recombinantes</term><term>Récepteurs viraux</term><term>Sous-type H7N9 du virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>Influenza A Virus, H7N9 Subtype</term></keywords><keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Sous-type H7N9 du virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="transmission" xml:lang="en"><term>Influenza in Birds</term><term>Influenza, Human</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Grippe chez les oiseaux</term><term>Grippe humaine</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Influenza in Birds</term><term>Influenza, Human</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Binding Sites</term><term>Birds</term><term>Carbohydrate Conformation</term><term>Crystallography, X-Ray</term><term>Humans</term><term>Ligands</term><term>Microarray Analysis</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Mutation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse sur microréseau</term><term>Animaux</term><term>Conformation des glucides</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Grippe chez les oiseaux</term><term>Grippe humaine</term><term>Humains</term><term>Ligands</term><term>Modèles moléculaires</term><term>Mutation</term><term>Oiseaux</term><term>Polyosides</term><term>Protéines recombinantes</term><term>Récepteurs viraux</term><term>Sites de fixation</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="P1">The 2013 outbreak of avian-origin H7N9 influenza in eastern China has raised concerns about its ability to transmit in the human population. The hemagglutinin glycoprotein of most human H7N9 viruses carries Leu226, a residue linked to adaptation of H2N2 and H3N2 pandemic viruses to human receptors. However, glycan array analysis of the H7 hemagglutinin reveals negligible binding to human-like α2-6-linked receptors and strong preference for a subset of avian-like α2-3-linked glycans recognized by all avian H7 viruses. Crystal structures of H7N9 hemagglutinin and six hemagglutinin-glycan complexes have elucidated the structural basis for preferential recognition of avian-like receptors. These findings suggest that the current human H7N9 viruses are poorly adapted for efficient human-to-human transmission.</p></div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Californie</li></region></list><tree><country name="États-Unis"><region name="Californie"><name sortKey="Xu, Rui" sort="Xu, Rui" uniqKey="Xu R" first="Rui" last="Xu">Rui Xu</name></region><name sortKey="De Vries, Robert P" sort="De Vries, Robert P" uniqKey="De Vries R" first="Robert P." last="De Vries">Robert P. De Vries</name><name sortKey="De Vries, Robert P" sort="De Vries, Robert P" uniqKey="De Vries R" first="Robert P." last="De Vries">Robert P. De Vries</name><name sortKey="Mcbride, Ryan" sort="Mcbride, Ryan" uniqKey="Mcbride R" first="Ryan" last="Mcbride">Ryan Mcbride</name><name sortKey="Mcbride, Ryan" sort="Mcbride, Ryan" uniqKey="Mcbride R" first="Ryan" last="Mcbride">Ryan Mcbride</name><name sortKey="Nycholat, Corwin M" sort="Nycholat, Corwin M" uniqKey="Nycholat C" first="Corwin M." last="Nycholat">Corwin M. Nycholat</name><name sortKey="Nycholat, Corwin M" sort="Nycholat, Corwin M" uniqKey="Nycholat C" first="Corwin M." last="Nycholat">Corwin M. Nycholat</name><name sortKey="Paulson, James C" sort="Paulson, James C" uniqKey="Paulson J" first="James C." last="Paulson">James C. Paulson</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="Wilson, Ian A" sort="Wilson, Ian A" uniqKey="Wilson I" first="Ian A." last="Wilson">Ian A. Wilson</name><name sortKey="Yu, Wenli" sort="Yu, Wenli" uniqKey="Yu W" first="Wenli" last="Yu">Wenli Yu</name><name sortKey="Zhu, Xueyong" sort="Zhu, Xueyong" uniqKey="Zhu X" first="Xueyong" last="Zhu">Xueyong Zhu</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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