Receptor Specificity and Transmission of H2N2 Subtype Viruses Isolated from the Pandemic of 1957
Identifieur interne : 000B11 ( Pmc/Curation ); précédent : 000B10; suivant : 000B12Receptor Specificity and Transmission of H2N2 Subtype Viruses Isolated from the Pandemic of 1957
Auteurs : Claudia Pappas [États-Unis] ; Karthik Viswanathan [États-Unis] ; Aarthi Chandrasekaran [États-Unis] ; Rahul Raman [États-Unis] ; Jacqueline M. Katz [États-Unis] ; Ram Sasisekharan [États-Unis] ; Terrence M. Tumpey [États-Unis]Source :
- PLoS ONE [ 1932-6203 ] ; 2010.
Abstract
Influenza viruses of the H2N2 subtype have not circulated among humans in over 40 years. The occasional isolation of avian H2 strains from swine and avian species coupled with waning population immunity to H2 hemagglutinin (HA) warrants investigation of this subtype due to its pandemic potential. In this study we examined the transmissibility of representative human H2N2 viruses, A/Albany/6/58 (Alb/58) and A/El Salvador/2/57 (ElSalv/57), isolated during the 1957/58 pandemic, in the ferret model. The receptor binding properties of these H2N2 viruses was analyzed using dose-dependent direct glycan array-binding assays. Alb/58 virus, which contains the 226L/228S amino acid combination in the HA and displayed dual binding to both alpha 2,6 and alpha 2,3 glycan receptors, transmitted efficiently to naïve ferrets by respiratory droplets. Inefficient transmission was observed with ElSalv/57 virus, which contains the 226Q/228G amino acid combination and preferentially binds alpha 2,3 over alpha 2,6 glycan receptors. However, a unique transmission event with the ElSalv/57 virus occurred which produced a 226L/228G H2N2 natural variant virus that displayed an increase in binding specificity to alpha 2,6 glycan receptors and enhanced respiratory droplet transmissibility. Our studies provide a correlation between binding affinity to glycan receptors with terminal alpha 2,6-linked sialic acid and the efficiency of respiratory droplet transmission for pandemic H2N2 influenza viruses.
Url:
DOI: 10.1371/journal.pone.0011158
PubMed: 20574518
PubMed Central: 2888575
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Katz</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Influenza Division, Centers for Disease Control and Prevention, Atlanta, Georgia, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Influenza Division, Centers for Disease Control and Prevention, Atlanta, Georgia</wicri:regionArea></affiliation></author><author><name sortKey="Sasisekharan, Ram" sort="Sasisekharan, Ram" uniqKey="Sasisekharan R" first="Ram" last="Sasisekharan">Ram Sasisekharan</name><affiliation wicri:level="1"><nlm:aff id="aff2"><addr-line>Harvard-Massachusetts Institute of Technology Division of Health Sciences and Technology, Koch Institute of Integrative Cancer Research, Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Harvard-Massachusetts Institute of Technology Division of Health Sciences and Technology, Koch Institute of Integrative Cancer Research, Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts</wicri:regionArea></affiliation></author><author><name sortKey="Tumpey, Terrence M" sort="Tumpey, Terrence M" uniqKey="Tumpey T" first="Terrence M." last="Tumpey">Terrence M. Tumpey</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Influenza Division, Centers for Disease Control and Prevention, Atlanta, Georgia, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Influenza Division, Centers for Disease Control and Prevention, Atlanta, Georgia</wicri:regionArea></affiliation></author></analytic><series><title level="j">PLoS ONE</title><idno type="eISSN">1932-6203</idno><imprint><date when="2010">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Influenza viruses of the H2N2 subtype have not circulated among humans in over 40 years. The occasional isolation of avian H2 strains from swine and avian species coupled with waning population immunity to H2 hemagglutinin (HA) warrants investigation of this subtype due to its pandemic potential. In this study we examined the transmissibility of representative human H2N2 viruses, A/Albany/6/58 (Alb/58) and A/El Salvador/2/57 (ElSalv/57), isolated during the 1957/58 pandemic, in the ferret model. The receptor binding properties of these H2N2 viruses was analyzed using dose-dependent direct glycan array-binding assays. Alb/58 virus, which contains the 226L/228S amino acid combination in the HA and displayed dual binding to both alpha 2,6 and alpha 2,3 glycan receptors, transmitted efficiently to naïve ferrets by respiratory droplets. Inefficient transmission was observed with ElSalv/57 virus, which contains the 226Q/228G amino acid combination and preferentially binds alpha 2,3 over alpha 2,6 glycan receptors. However, a unique transmission event with the ElSalv/57 virus occurred which produced a 226L/228G H2N2 natural variant virus that displayed an increase in binding specificity to alpha 2,6 glycan receptors and enhanced respiratory droplet transmissibility. Our studies provide a correlation between binding affinity to glycan receptors with terminal alpha 2,6-linked sialic acid and the efficiency of respiratory droplet transmission for pandemic H2N2 influenza viruses.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Fouchier, Ra" uniqKey="Fouchier R">RA Fouchier</name></author><author><name sortKey="Munster, V" uniqKey="Munster V">V Munster</name></author><author><name sortKey="Wallensten, A" uniqKey="Wallensten A">A Wallensten</name></author><author><name sortKey="Bestebroer, Tm" uniqKey="Bestebroer T">TM Bestebroer</name></author><author><name sortKey="Herfst, S" uniqKey="Herfst S">S Herfst</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Simonsen, L" uniqKey="Simonsen L">L Simonsen</name></author><author><name sortKey="Clarke, Mj" uniqKey="Clarke M">MJ Clarke</name></author><author><name sortKey="Schonberger, Lb" uniqKey="Schonberger L">LB 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<front><journal-meta><journal-id journal-id-type="nlm-ta">PLoS One</journal-id><journal-id journal-id-type="iso-abbrev">PLoS ONE</journal-id><journal-id journal-id-type="publisher-id">plos</journal-id><journal-id journal-id-type="pmc">plosone</journal-id><journal-title-group><journal-title>PLoS ONE</journal-title></journal-title-group><issn pub-type="epub">1932-6203</issn><publisher><publisher-name>Public Library of Science</publisher-name><publisher-loc>San Francisco, USA</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">20574518</article-id><article-id pub-id-type="pmc">2888575</article-id><article-id pub-id-type="publisher-id">10-PONE-RA-15604R1</article-id><article-id pub-id-type="doi">10.1371/journal.pone.0011158</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group><subj-group subj-group-type="Discipline"><subject>Infectious Diseases</subject><subject>Virology</subject><subject>Microbiology/Cellular Microbiology and Pathogenesis</subject><subject>Virology/Animal Models of Infection</subject><subject>Infectious Diseases/Viral Infections</subject></subj-group></article-categories><title-group><article-title>Receptor Specificity and Transmission of H2N2 Subtype Viruses Isolated from the Pandemic of 1957</article-title><alt-title alt-title-type="running-head">Pandemic H2N2 Transmission</alt-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Pappas</surname><given-names>Claudia</given-names></name><xref ref-type="aff" rid="aff1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Viswanathan</surname><given-names>Karthik</given-names></name><xref ref-type="aff" rid="aff2"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Chandrasekaran</surname><given-names>Aarthi</given-names></name><xref ref-type="aff" rid="aff2"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Raman</surname><given-names>Rahul</given-names></name><xref ref-type="aff" rid="aff2"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Katz</surname><given-names>Jacqueline M.</given-names></name><xref ref-type="aff" rid="aff1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Sasisekharan</surname><given-names>Ram</given-names></name><xref ref-type="aff" rid="aff2"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Tumpey</surname><given-names>Terrence M.</given-names></name><xref ref-type="aff" rid="aff1"><sup>1</sup></xref><xref ref-type="corresp" rid="cor1"><sup>*</sup></xref></contrib></contrib-group><aff id="aff1"><label>1</label><addr-line>Influenza Division, Centers for Disease Control and Prevention, Atlanta, Georgia, United States of America</addr-line></aff><aff id="aff2"><label>2</label><addr-line>Harvard-Massachusetts Institute of Technology Division of Health Sciences and Technology, Koch Institute of Integrative Cancer Research, Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts, United States of America</addr-line></aff><contrib-group><contrib contrib-type="editor"><name><surname>Zhang</surname><given-names>Linqi</given-names></name><role>Editor</role><xref ref-type="aff" rid="edit1"></xref></contrib></contrib-group><aff id="edit1">Tsinghua University, China</aff><author-notes><corresp id="cor1">* E-mail: <email>tft9@cdc.gov</email></corresp><fn fn-type="con"><p>Conceived and designed the experiments: CP KV AC RR JMK RS TMT. Performed the experiments: CP KV AC RR TMT. Analyzed the data: CP KV AC RR JMK RS TMT. Contributed reagents/materials/analysis tools: CP KV AC RR JMK RS TMT. Wrote the paper: CP RR JMK RS TMT.</p></fn></author-notes><pub-date pub-type="collection"><year>2010</year></pub-date><pub-date pub-type="epub"><day>21</day><month>6</month><year>2010</year></pub-date><volume>5</volume><issue>6</issue><elocation-id>e11158</elocation-id><history><date date-type="received"><day>18</day><month>1</month><year>2010</year></date><date date-type="accepted"><day>13</day><month>5</month><year>2010</year></date></history><permissions><copyright-statement>This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.</copyright-statement><copyright-year>2010</copyright-year><license xlink:href="https://creativecommons.org/publicdomain/zero/1.0/"><license-p>This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.</license-p></license></permissions><abstract><p>Influenza viruses of the H2N2 subtype have not circulated among humans in over 40 years. The occasional isolation of avian H2 strains from swine and avian species coupled with waning population immunity to H2 hemagglutinin (HA) warrants investigation of this subtype due to its pandemic potential. In this study we examined the transmissibility of representative human H2N2 viruses, A/Albany/6/58 (Alb/58) and A/El Salvador/2/57 (ElSalv/57), isolated during the 1957/58 pandemic, in the ferret model. The receptor binding properties of these H2N2 viruses was analyzed using dose-dependent direct glycan array-binding assays. Alb/58 virus, which contains the 226L/228S amino acid combination in the HA and displayed dual binding to both alpha 2,6 and alpha 2,3 glycan receptors, transmitted efficiently to naïve ferrets by respiratory droplets. Inefficient transmission was observed with ElSalv/57 virus, which contains the 226Q/228G amino acid combination and preferentially binds alpha 2,3 over alpha 2,6 glycan receptors. However, a unique transmission event with the ElSalv/57 virus occurred which produced a 226L/228G H2N2 natural variant virus that displayed an increase in binding specificity to alpha 2,6 glycan receptors and enhanced respiratory droplet transmissibility. Our studies provide a correlation between binding affinity to glycan receptors with terminal alpha 2,6-linked sialic acid and the efficiency of respiratory droplet transmission for pandemic H2N2 influenza viruses.</p></abstract><counts><page-count count="10"></page-count></counts></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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