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Three mutations switch H7N9 influenza to human-type receptor specificity.

Identifieur interne : 000037 ( PubMed/Curation ); précédent : 000036; suivant : 000038

Three mutations switch H7N9 influenza to human-type receptor specificity.

Auteurs : Robert P. De Vries [États-Unis] ; Wenjie Peng [États-Unis] ; Oliver C. Grant [États-Unis] ; Andrew J. Thompson [États-Unis] ; Xueyong Zhu [États-Unis] ; Kim M. Bouwman [Pays-Bas] ; Alba T Torrents De La Pena [Pays-Bas] ; Marielle J. Van Breemen [Pays-Bas] ; Iresha N. Ambepitiya Wickramasinghe [Pays-Bas] ; Cornelis A M. De Haan [Pays-Bas] ; Wenli Yu [États-Unis] ; Ryan Mcbride [États-Unis] ; Rogier W. Sanders [Pays-Bas] ; Robert J. Woods [États-Unis] ; Monique H. Verheije [Pays-Bas] ; Ian A. Wilson [États-Unis] ; James C. Paulson [États-Unis]

Source :

RBID : pubmed:28617868

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English descriptors

Abstract

The avian H7N9 influenza outbreak in 2013 resulted from an unprecedented incidence of influenza transmission to humans from infected poultry. The majority of human H7N9 isolates contained a hemagglutinin (HA) mutation (Q226L) that has previously been associated with a switch in receptor specificity from avian-type (NeuAcα2-3Gal) to human-type (NeuAcα2-6Gal), as documented for the avian progenitors of the 1957 (H2N2) and 1968 (H3N2) human influenza pandemic viruses. While this raised concern that the H7N9 virus was adapting to humans, the mutation was not sufficient to switch the receptor specificity of H7N9, and has not resulted in sustained transmission in humans. To determine if the H7 HA was capable of acquiring human-type receptor specificity, we conducted mutation analyses. Remarkably, three amino acid mutations conferred a switch in specificity for human-type receptors that resembled the specificity of the 2009 human H1 pandemic virus, and promoted binding to human trachea epithelial cells.

DOI: 10.1371/journal.ppat.1006390
PubMed: 28617868

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pubmed:28617868

Le document en format XML

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<nlm:affiliation>Department of Medical Microbiology, Academic Medical Center, University of Amsterdam, AZ Amsterdam, The Netherlands.</nlm:affiliation>
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<term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Hemagglutinin Glycoproteins, Influenza Virus (chemistry)</term>
<term>Hemagglutinin Glycoproteins, Influenza Virus (genetics)</term>
<term>Hemagglutinin Glycoproteins, Influenza Virus (metabolism)</term>
<term>Host Specificity</term>
<term>Humans</term>
<term>Influenza A Virus, H3N2 Subtype (chemistry)</term>
<term>Influenza A Virus, H3N2 Subtype (genetics)</term>
<term>Influenza A Virus, H3N2 Subtype (metabolism)</term>
<term>Influenza A Virus, H7N9 Subtype (chemistry)</term>
<term>Influenza A Virus, H7N9 Subtype (genetics)</term>
<term>Influenza A Virus, H7N9 Subtype (metabolism)</term>
<term>Influenza in Birds (genetics)</term>
<term>Influenza in Birds (metabolism)</term>
<term>Influenza in Birds (virology)</term>
<term>Influenza, Human (genetics)</term>
<term>Influenza, Human (metabolism)</term>
<term>Influenza, Human (virology)</term>
<term>Molecular Sequence Data</term>
<term>Mutation</term>
<term>Poultry</term>
<term>Poultry Diseases (genetics)</term>
<term>Poultry Diseases (metabolism)</term>
<term>Poultry Diseases (virology)</term>
<term>Protein Binding</term>
<term>Receptors, Virus (genetics)</term>
<term>Receptors, Virus (metabolism)</term>
<term>Sequence Alignment</term>
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<term>Alignement de séquences</term>
<term>Animaux</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 chez les oiseaux (génétique)</term>
<term>Grippe chez les oiseaux (métabolisme)</term>
<term>Grippe chez les oiseaux (virologie)</term>
<term>Grippe humaine (génétique)</term>
<term>Grippe humaine (métabolisme)</term>
<term>Grippe humaine (virologie)</term>
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<term>Liaison aux protéines</term>
<term>Maladies de la volaille (génétique)</term>
<term>Maladies de la volaille (métabolisme)</term>
<term>Maladies de la volaille (virologie)</term>
<term>Mutation</term>
<term>Récepteurs viraux (génétique)</term>
<term>Récepteurs viraux (métabolisme)</term>
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<term>Sous-type H3N2 du virus de la grippe A (génétique)</term>
<term>Sous-type H3N2 du virus de la grippe A (métabolisme)</term>
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<term>Sous-type H7N9 du virus de la grippe A (métabolisme)</term>
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<term>Séquence d'acides aminés</term>
<term>Volaille</term>
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<term>Influenza, Human</term>
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<term>Grippe humaine</term>
<term>Maladies de la volaille</term>
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<term>Sous-type H7N9 du virus de la grippe A</term>
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<term>Influenza A Virus, H7N9 Subtype</term>
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<term>Influenza, Human</term>
<term>Poultry Diseases</term>
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<term>Grippe humaine</term>
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<term>Récepteurs viraux</term>
<term>Sous-type H3N2 du virus de la grippe A</term>
<term>Sous-type H7N9 du virus de la grippe A</term>
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<term>Grippe humaine</term>
<term>Maladies de la volaille</term>
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<term>Influenza in Birds</term>
<term>Influenza, Human</term>
<term>Poultry Diseases</term>
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<term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Host Specificity</term>
<term>Humans</term>
<term>Molecular Sequence Data</term>
<term>Mutation</term>
<term>Poultry</term>
<term>Protein Binding</term>
<term>Sequence Alignment</term>
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<term>Alignement de séquences</term>
<term>Animaux</term>
<term>Données de séquences moléculaires</term>
<term>Glycoprotéine hémagglutinine du virus influenza</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Mutation</term>
<term>Sous-type H3N2 du virus de la grippe A</term>
<term>Sous-type H7N9 du virus de la grippe A</term>
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<div type="abstract" xml:lang="en">The avian H7N9 influenza outbreak in 2013 resulted from an unprecedented incidence of influenza transmission to humans from infected poultry. The majority of human H7N9 isolates contained a hemagglutinin (HA) mutation (Q226L) that has previously been associated with a switch in receptor specificity from avian-type (NeuAcα2-3Gal) to human-type (NeuAcα2-6Gal), as documented for the avian progenitors of the 1957 (H2N2) and 1968 (H3N2) human influenza pandemic viruses. While this raised concern that the H7N9 virus was adapting to humans, the mutation was not sufficient to switch the receptor specificity of H7N9, and has not resulted in sustained transmission in humans. To determine if the H7 HA was capable of acquiring human-type receptor specificity, we conducted mutation analyses. Remarkably, three amino acid mutations conferred a switch in specificity for human-type receptors that resembled the specificity of the 2009 human H1 pandemic virus, and promoted binding to human trachea epithelial cells.</div>
</front>
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<Month>09</Month>
<Day>21</Day>
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<DateRevised>
<Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
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<Volume>13</Volume>
<Issue>6</Issue>
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<Year>2017</Year>
<Month>Jun</Month>
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<Title>PLoS pathogens</Title>
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<ArticleTitle>Three mutations switch H7N9 influenza to human-type receptor specificity.</ArticleTitle>
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<AbstractText>The avian H7N9 influenza outbreak in 2013 resulted from an unprecedented incidence of influenza transmission to humans from infected poultry. The majority of human H7N9 isolates contained a hemagglutinin (HA) mutation (Q226L) that has previously been associated with a switch in receptor specificity from avian-type (NeuAcα2-3Gal) to human-type (NeuAcα2-6Gal), as documented for the avian progenitors of the 1957 (H2N2) and 1968 (H3N2) human influenza pandemic viruses. While this raised concern that the H7N9 virus was adapting to humans, the mutation was not sufficient to switch the receptor specificity of H7N9, and has not resulted in sustained transmission in humans. To determine if the H7 HA was capable of acquiring human-type receptor specificity, we conducted mutation analyses. Remarkably, three amino acid mutations conferred a switch in specificity for human-type receptors that resembled the specificity of the 2009 human H1 pandemic virus, and promoted binding to human trachea epithelial cells.</AbstractText>
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<LastName>de Vries</LastName>
<ForeName>Robert P</ForeName>
<Initials>RP</Initials>
<AffiliationInfo>
<Affiliation>Departments of Molecular Medicine, & Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA, United States of America.</Affiliation>
</AffiliationInfo>
<AffiliationInfo>
<Affiliation>Department of Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, CG Utrecht, The Netherlands.</Affiliation>
</AffiliationInfo>
</Author>
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<LastName>Peng</LastName>
<ForeName>Wenjie</ForeName>
<Initials>W</Initials>
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<AffiliationInfo>
<Affiliation>Departments of Molecular Medicine, & Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA, United States of America.</Affiliation>
</AffiliationInfo>
</Author>
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<LastName>Grant</LastName>
<ForeName>Oliver C</ForeName>
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<Affiliation>Complex Carbohydrate Research Center, University of Georgia, Athens, GA, United States of America.</Affiliation>
</AffiliationInfo>
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<LastName>Thompson</LastName>
<ForeName>Andrew J</ForeName>
<Initials>AJ</Initials>
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<Affiliation>Departments of Molecular Medicine, & Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA, United States of America.</Affiliation>
</AffiliationInfo>
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<LastName>Zhu</LastName>
<ForeName>Xueyong</ForeName>
<Initials>X</Initials>
<AffiliationInfo>
<Affiliation>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, United States of America.</Affiliation>
</AffiliationInfo>
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<LastName>Bouwman</LastName>
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<LastName>van Breemen</LastName>
<ForeName>Marielle J</ForeName>
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</AffiliationInfo>
</Author>
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<LastName>Ambepitiya Wickramasinghe</LastName>
<ForeName>Iresha N</ForeName>
<Initials>IN</Initials>
<AffiliationInfo>
<Affiliation>Pathology Division, Department of Pathobiology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, CL Utrecht, The Netherlands.</Affiliation>
</AffiliationInfo>
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<ForeName>Cornelis A M</ForeName>
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<AffiliationInfo>
<Affiliation>Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1,CL Utrecht, The Netherlands.</Affiliation>
</AffiliationInfo>
</Author>
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<LastName>Yu</LastName>
<ForeName>Wenli</ForeName>
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<AffiliationInfo>
<Affiliation>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, United States of America.</Affiliation>
</AffiliationInfo>
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<LastName>McBride</LastName>
<ForeName>Ryan</ForeName>
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<AffiliationInfo>
<Affiliation>Departments of Molecular Medicine, & Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA, United States of America.</Affiliation>
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<LastName>Sanders</LastName>
<ForeName>Rogier W</ForeName>
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<AffiliationInfo>
<Affiliation>Department of Medical Microbiology, Academic Medical Center, University of Amsterdam, AZ Amsterdam, The Netherlands.</Affiliation>
</AffiliationInfo>
<AffiliationInfo>
<Affiliation>Department of Microbiology and Immunology, Weil Medical College of Cornell University, New York, NY, United States of America.</Affiliation>
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<Affiliation>Pathology Division, Department of Pathobiology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, CL Utrecht, The Netherlands.</Affiliation>
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<LastName>Wilson</LastName>
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<AffiliationInfo>
<Affiliation>Departments of Molecular Medicine, & Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA, United States of America.</Affiliation>
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<Acronym>CA</Acronym>
<Agency>NCI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant>
<GrantID>R01 GM100058</GrantID>
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