Unique Structural Features of Influenza Virus H15 Hemagglutinin
Identifieur interne : 000697 ( Pmc/Corpus ); précédent : 000696; suivant : 000698Unique Structural Features of Influenza Virus H15 Hemagglutinin
Auteurs : Netanel Tzarum ; Ryan Mcbride ; Corwin M. Nycholat ; Wenjie Peng ; James C. Paulson ; Ian A. WilsonSource :
- Journal of Virology [ 0022-538X ] ; 2017.
Abstract
Influenza A H15 viruses are members of a subgroup (H7-H10-H15) of group 2 hemagglutinin (HA) subtypes that include H7N9 and H10N8 viruses that were isolated from humans during 2013. The isolation of avian H15 viruses is, however, quite rare and, until recently, geographically restricted to wild shorebirds and waterfowl in Australia. The HAs of H15 viruses contain an insertion in the 150-loop (loop beginning at position 150) of the receptor-binding site common to this subgroup and a unique insertion in the 260-loop compared to any other subtype. Here, we show that the H15 HA has a high preference for avian receptor analogs by glycan array analyses. The H15 HA crystal structure reveals that it is structurally closest to H7N9 HA, but the head domain of the H15 trimer is wider than all other HAs due to a tilt and opening of the HA1 subunits of the head domain. The extended 150-loop of the H15 HA retains the conserved conformation as in H7 and H10 HAs. Furthermore, the elongated 260-loop increases the exposed HA surface and can contribute to antigenic variation in H15 HAs. Since avian-origin H15 HA viruses have been shown to cause enhanced disease in mammalian models, further characterization and immune surveillance of H15 viruses are warranted.
Url:
DOI: 10.1128/JVI.00046-17
PubMed: 28404848
PubMed Central: 5446636
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PMC:5446636Le document en format XML
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<series><title level="j">Journal of Virology</title>
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<front><div type="abstract" xml:lang="en"><title>ABSTRACT</title>
<p>Influenza A H15 viruses are members of a subgroup (H7-H10-H15) of group 2 hemagglutinin (HA) subtypes that include H7N9 and H10N8 viruses that were isolated from humans during 2013. The isolation of avian H15 viruses is, however, quite rare and, until recently, geographically restricted to wild shorebirds and waterfowl in Australia. The HAs of H15 viruses contain an insertion in the 150-loop (loop beginning at position 150) of the receptor-binding site common to this subgroup and a unique insertion in the 260-loop compared to any other subtype. Here, we show that the H15 HA has a high preference for avian receptor analogs by glycan array analyses. The H15 HA crystal structure reveals that it is structurally closest to H7N9 HA, but the head domain of the H15 trimer is wider than all other HAs due to a tilt and opening of the HA1 subunits of the head domain. The extended 150-loop of the H15 HA retains the conserved conformation as in H7 and H10 HAs. Furthermore, the elongated 260-loop increases the exposed HA surface and can contribute to antigenic variation in H15 HAs. Since avian-origin H15 HA viruses have been shown to cause enhanced disease in mammalian models, further characterization and immune surveillance of H15 viruses are warranted.</p>
<p><bold>IMPORTANCE</bold>
In the last 2 decades, an apparent increase has been reported for cases of human infection by emerging avian influenza A virus subtypes, including H7N9 and H10N8 viruses isolated during 2013. H15 is the other member of the subgroup of influenza A virus group 2 hemagglutinins (HAs) that also include H7 and H10. H15 viruses have been restricted to Australia, but recent isolation of H15 viruses in western Siberia suggests that they could be spread more globally via the avian flyways that converge and emanate from this region. Here we report on characterization of the three-dimensional structure and receptor specificity of the H15 hemagglutinin, revealing distinct features and specificities that can aid in global surveillance of such viruses for potential spread and emerging threat to the human population.</p>
</div>
</front>
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<pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Virol</journal-id>
<journal-id journal-id-type="iso-abbrev">J. Virol</journal-id>
<journal-id journal-id-type="hwp">jvi</journal-id>
<journal-id journal-id-type="pmc">jvi</journal-id>
<journal-id journal-id-type="publisher-id">JVI</journal-id>
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<issn pub-type="epub">1098-5514</issn>
<publisher><publisher-name>American Society for Microbiology</publisher-name>
<publisher-loc>1752 N St., N.W., Washington, DC</publisher-loc>
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<article-id pub-id-type="doi">10.1128/JVI.00046-17</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Virus-Cell Interactions</subject>
</subj-group>
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<title-group><article-title>Unique Structural Features of Influenza Virus H15 Hemagglutinin</article-title>
<alt-title alt-title-type="running-head">Unique Structural Features of Influenza Virus H15 HA</alt-title>
<alt-title alt-title-type="short-authors">Tzarum et al.</alt-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Tzarum</surname>
<given-names>Netanel</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>a</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>McBride</surname>
<given-names>Ryan</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>b</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Nycholat</surname>
<given-names>Corwin M.</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>b</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Peng</surname>
<given-names>Wenjie</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>b</sup>
</xref>
<xref ref-type="aff" rid="aff3"><sup>c</sup>
</xref>
</contrib>
<contrib contrib-type="author" corresp="yes"><name><surname>Paulson</surname>
<given-names>James C.</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>b</sup>
</xref>
<xref ref-type="aff" rid="aff3"><sup>c</sup>
</xref>
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<contrib contrib-type="author" corresp="yes"><name><surname>Wilson</surname>
<given-names>Ian A.</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>a</sup>
</xref>
<xref ref-type="aff" rid="aff4"><sup>d</sup>
</xref>
</contrib>
<aff id="aff1"><label>a</label>
Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, USA</aff>
<aff id="aff2"><label>b</label>
Department of Molecular Medicine, The Scripps Research Institute, La Jolla, California, USA</aff>
<aff id="aff3"><label>c</label>
Department of Immunology and Microbiology, The Scripps Research Institute, La Jolla, California, USA</aff>
<aff id="aff4"><label>d</label>
Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California, USA</aff>
</contrib-group>
<contrib-group><contrib contrib-type="editor"><name><surname>García-Sastre</surname>
<given-names>Adolfo</given-names>
</name>
<role>Editor</role>
<aff>Icahn School of Medicine at Mount Sinai</aff>
</contrib>
</contrib-group>
<author-notes><corresp id="cor1">Address correspondence to James C. Paulson, <email>jpaulson@scripps.edu</email>
, or Ian A. Wilson, <email>wilson@scripps.edu</email>
.</corresp>
<fn fn-type="other"><p><bold>Citation</bold>
Tzarum N, McBride R, Nycholat CM, Peng W, Paulson JC, Wilson IA. 2017. Unique structural features of influenza virus H15 hemagglutinin. J Virol 91:e00046-17. <ext-link ext-link-type="uri" xlink:href="https://doi.org/10.1128/JVI.00046-17">https://doi.org/10.1128/JVI.00046-17</ext-link>
.</p>
</fn>
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<pub-date pub-type="epreprint"><day>12</day>
<month>4</month>
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<pub-date pub-type="epub"><day>26</day>
<month>5</month>
<year>2017</year>
</pub-date>
<pub-date pub-type="collection"><day>15</day>
<month>6</month>
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<volume>91</volume>
<issue>12</issue>
<elocation-id>e00046-17</elocation-id>
<history><date date-type="received"><day>9</day>
<month>1</month>
<year>2017</year>
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<date date-type="accepted"><day>4</day>
<month>4</month>
<year>2017</year>
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<permissions><copyright-statement>Copyright © 2017 American Society for Microbiology.</copyright-statement>
<copyright-year>2017</copyright-year>
<copyright-holder>American Society for Microbiology</copyright-holder>
<license license-type="asm" xlink:href="https://doi.org/10.1128/ASMCopyrightv1"><license-p><ext-link ext-link-type="uri" xlink:href="https://doi.org/10.1128/ASMCopyrightv1">All Rights Reserved</ext-link>
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<abstract><title>ABSTRACT</title>
<p>Influenza A H15 viruses are members of a subgroup (H7-H10-H15) of group 2 hemagglutinin (HA) subtypes that include H7N9 and H10N8 viruses that were isolated from humans during 2013. The isolation of avian H15 viruses is, however, quite rare and, until recently, geographically restricted to wild shorebirds and waterfowl in Australia. The HAs of H15 viruses contain an insertion in the 150-loop (loop beginning at position 150) of the receptor-binding site common to this subgroup and a unique insertion in the 260-loop compared to any other subtype. Here, we show that the H15 HA has a high preference for avian receptor analogs by glycan array analyses. The H15 HA crystal structure reveals that it is structurally closest to H7N9 HA, but the head domain of the H15 trimer is wider than all other HAs due to a tilt and opening of the HA1 subunits of the head domain. The extended 150-loop of the H15 HA retains the conserved conformation as in H7 and H10 HAs. Furthermore, the elongated 260-loop increases the exposed HA surface and can contribute to antigenic variation in H15 HAs. Since avian-origin H15 HA viruses have been shown to cause enhanced disease in mammalian models, further characterization and immune surveillance of H15 viruses are warranted.</p>
<p><bold>IMPORTANCE</bold>
In the last 2 decades, an apparent increase has been reported for cases of human infection by emerging avian influenza A virus subtypes, including H7N9 and H10N8 viruses isolated during 2013. H15 is the other member of the subgroup of influenza A virus group 2 hemagglutinins (HAs) that also include H7 and H10. H15 viruses have been restricted to Australia, but recent isolation of H15 viruses in western Siberia suggests that they could be spread more globally via the avian flyways that converge and emanate from this region. Here we report on characterization of the three-dimensional structure and receptor specificity of the H15 hemagglutinin, revealing distinct features and specificities that can aid in global surveillance of such viruses for potential spread and emerging threat to the human population.</p>
</abstract>
<kwd-group><title>KEYWORDS</title>
<kwd>influenza virus</kwd>
<kwd>H15 subtype</kwd>
<kwd>receptor binding</kwd>
<kwd>glycan arrays</kwd>
<kwd>X-ray crystallography</kwd>
</kwd-group>
<funding-group><award-group id="award1"><funding-source id="gs1">DH | National Institute for Health Research (NIHR)
<named-content content-type="funder-id">https://doi.org/10.13039/501100000272</named-content>
</funding-source>
<award-id rid="gs1">R56 AI117675</award-id>
<principal-award-recipient>Ian A. Wilson</principal-award-recipient>
</award-group>
<award-group id="award2"><funding-source id="gs2">DH | National Institute for Health Research (NIHR)
<named-content content-type="funder-id">https://doi.org/10.13039/501100000272</named-content>
</funding-source>
<award-id rid="gs2">R01 AI114730</award-id>
<principal-award-recipient>James C. Paulson</principal-award-recipient>
</award-group>
<award-group id="award3"><funding-source id="gs3">DH | National Institute for Health Research (NIHR)
<named-content content-type="funder-id">https://doi.org/10.13039/501100000272</named-content>
</funding-source>
<award-id rid="gs3">U54 GM094586</award-id>
<principal-award-recipient>Ian A. Wilson</principal-award-recipient>
</award-group>
</funding-group>
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<custom-meta-group><custom-meta><meta-name>cover-date</meta-name>
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