The 150-loop restricts the host specificity of human H10N8 influenza virus
Identifieur interne : 000834 ( Pmc/Corpus ); précédent : 000833; suivant : 000835The 150-loop restricts the host specificity of human H10N8 influenza virus
Auteurs : Netanel Tzarum ; Robert P. De Vries ; Wenjie Peng ; Andrew J. Thompson ; Kim Bouwman ; Ryan Mcbride ; Wenli Yu ; Xueyong Zhu ; Monique H. Verheije ; James C. Paulson ; Ian A. WilsonSource :
- Cell reports [ 2211-1247 ] ; 2017.
Abstract
Adaptation of influenza A viruses to new hosts are rare events, but are the basis for emergence of new influenza pandemics in the human population. Thus, understanding the processes involved in such events is critical for anticipating potential pandemic threats. In 2013, the first case of human infection by an avian H10N8 virus was reported, yet the H10 HA maintains avian receptor specificity. However, the 150-loop of H10 HA, as well as related H7 and H15 subtypes, contains a two-residue insert that can potentially block human receptor binding. Mutation of the 150-loop on the background of Q226L and G228S mutations, which arose in the receptor-binding site of human pandemic H2 and H3 viruses, resulted in acquisition of human-type receptor specificity. Crystal structures of H10 HA mutants with human and avian receptors analogs, receptor binding studies, and tissue staining experiments illustrate the important role of the 150-loop in H10 receptor specificity.
Url:
DOI: 10.1016/j.celrep.2017.03.054
PubMed: 28402848
PubMed Central: 5452617
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PMC:5452617Le document en format XML
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<affiliation><nlm:aff id="A4">Department of Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, 3584 CG Utrecht, The Netherlands</nlm:aff>
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</affiliation>
<affiliation><nlm:aff id="A4">Department of Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, 3584 CG Utrecht, The Netherlands</nlm:aff>
</affiliation>
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<author><name sortKey="Peng, Wenjie" sort="Peng, Wenjie" uniqKey="Peng W" first="Wenjie" last="Peng">Wenjie Peng</name>
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<author><name sortKey="Thompson, Andrew J" sort="Thompson, Andrew J" uniqKey="Thompson A" first="Andrew J." last="Thompson">Andrew J. Thompson</name>
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</affiliation>
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</affiliation>
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</affiliation>
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<author><name sortKey="Yu, Wenli" sort="Yu, Wenli" uniqKey="Yu W" first="Wenli" last="Yu">Wenli Yu</name>
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</affiliation>
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<author><name sortKey="Zhu, Xueyong" sort="Zhu, Xueyong" uniqKey="Zhu X" first="Xueyong" last="Zhu">Xueyong Zhu</name>
<affiliation><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>
</affiliation>
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<author><name sortKey="Verheije, Monique H" sort="Verheije, Monique H" uniqKey="Verheije M" first="Monique H." last="Verheije">Monique H. Verheije</name>
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</affiliation>
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<author><name sortKey="Paulson, James C" sort="Paulson, James C" uniqKey="Paulson J" first="James C." last="Paulson">James C. Paulson</name>
<affiliation><nlm:aff id="A2">Department of Molecular Medicine and Dept. of Immunology and Microbiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA</nlm:aff>
</affiliation>
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<author><name sortKey="Wilson, Ian A" sort="Wilson, Ian A" uniqKey="Wilson I" first="Ian A." last="Wilson">Ian A. Wilson</name>
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</affiliation>
<affiliation><nlm:aff id="A3">Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA</nlm:aff>
</affiliation>
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<series><title level="j">Cell reports</title>
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<front><div type="abstract" xml:lang="en"><title>SUMMARY</title>
<p id="P1">Adaptation of influenza A viruses to new hosts are rare events, but are the basis for emergence of new influenza pandemics in the human population. Thus, understanding the processes involved in such events is critical for anticipating potential pandemic threats. In 2013, the first case of human infection by an avian H10N8 virus was reported, yet the H10 HA maintains avian receptor specificity. However, the 150-loop of H10 HA, as well as related H7 and H15 subtypes, contains a two-residue insert that can potentially block human receptor binding. Mutation of the 150-loop on the background of Q226L and G228S mutations, which arose in the receptor-binding site of human pandemic H2 and H3 viruses, resulted in acquisition of human-type receptor specificity. Crystal structures of H10 HA mutants with human and avian receptors analogs, receptor binding studies, and tissue staining experiments illustrate the important role of the 150-loop in H10 receptor specificity.</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>
<pmc-dir>properties manuscript</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-journal-id">101573691</journal-id>
<journal-id journal-id-type="pubmed-jr-id">39703</journal-id>
<journal-id journal-id-type="nlm-ta">Cell Rep</journal-id>
<journal-id journal-id-type="iso-abbrev">Cell Rep</journal-id>
<journal-title-group><journal-title>Cell reports</journal-title>
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<issn pub-type="epub">2211-1247</issn>
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<article-meta><article-id pub-id-type="pmid">28402848</article-id>
<article-id pub-id-type="pmc">5452617</article-id>
<article-id pub-id-type="doi">10.1016/j.celrep.2017.03.054</article-id>
<article-id pub-id-type="manuscript">NIHMS864988</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Article</subject>
</subj-group>
</article-categories>
<title-group><article-title>The 150-loop restricts the host specificity of human H10N8 influenza virus</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Tzarum</surname>
<given-names>Netanel</given-names>
</name>
<xref ref-type="aff" rid="A1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>de Vries</surname>
<given-names>Robert P.</given-names>
</name>
<xref ref-type="aff" rid="A2">2</xref>
<xref ref-type="aff" rid="A4">4</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Peng</surname>
<given-names>Wenjie</given-names>
</name>
<xref ref-type="aff" rid="A2">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Thompson</surname>
<given-names>Andrew J.</given-names>
</name>
<xref ref-type="aff" rid="A2">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Bouwman</surname>
<given-names>Kim</given-names>
</name>
<xref ref-type="aff" rid="A5">5</xref>
</contrib>
<contrib contrib-type="author"><name><surname>McBride</surname>
<given-names>Ryan</given-names>
</name>
<xref ref-type="aff" rid="A2">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Yu</surname>
<given-names>Wenli</given-names>
</name>
<xref ref-type="aff" rid="A1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Zhu</surname>
<given-names>Xueyong</given-names>
</name>
<xref ref-type="aff" rid="A1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Verheije</surname>
<given-names>Monique H.</given-names>
</name>
<xref ref-type="aff" rid="A5">5</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Paulson</surname>
<given-names>James C.</given-names>
</name>
<xref ref-type="aff" rid="A2">2</xref>
<xref rid="FN1" ref-type="author-notes">*</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Wilson</surname>
<given-names>Ian A.</given-names>
</name>
<xref ref-type="aff" rid="A1">1</xref>
<xref ref-type="aff" rid="A3">3</xref>
<xref rid="FN2" ref-type="author-notes">6</xref>
<xref rid="FN1" ref-type="author-notes">*</xref>
</contrib>
</contrib-group>
<aff id="A1"><label>1</label>
Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA</aff>
<aff id="A2"><label>2</label>
Department of Molecular Medicine and Dept. of Immunology and Microbiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA</aff>
<aff id="A3"><label>3</label>
Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA</aff>
<aff id="A4"><label>4</label>
Department of Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, 3584 CG Utrecht, The Netherlands</aff>
<aff id="A5"><label>5</label>
Pathology Division, Department of Pathobiology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, The Netherlands</aff>
<author-notes><corresp id="FN1"><label>*</label>
Correspondence: <email>wilson@scripps.edu</email>
, <email>jpaulson@scripps.edu</email>
</corresp>
<fn id="FN2"><label>6</label>
<p>Lead Contacts</p>
</fn>
</author-notes>
<pub-date pub-type="nihms-submitted"><day>3</day>
<month>4</month>
<year>2017</year>
</pub-date>
<pub-date pub-type="ppub"><day>11</day>
<month>4</month>
<year>2017</year>
</pub-date>
<pub-date pub-type="pmc-release"><day>11</day>
<month>4</month>
<year>2018</year>
</pub-date>
<volume>19</volume>
<issue>2</issue>
<fpage>235</fpage>
<lpage>245</lpage>
<pmc-comment>elocation-id from pubmed: 10.1016/j.celrep.2017.03.054</pmc-comment>
<abstract id="Abs1"><title>SUMMARY</title>
<p id="P1">Adaptation of influenza A viruses to new hosts are rare events, but are the basis for emergence of new influenza pandemics in the human population. Thus, understanding the processes involved in such events is critical for anticipating potential pandemic threats. In 2013, the first case of human infection by an avian H10N8 virus was reported, yet the H10 HA maintains avian receptor specificity. However, the 150-loop of H10 HA, as well as related H7 and H15 subtypes, contains a two-residue insert that can potentially block human receptor binding. Mutation of the 150-loop on the background of Q226L and G228S mutations, which arose in the receptor-binding site of human pandemic H2 and H3 viruses, resulted in acquisition of human-type receptor specificity. Crystal structures of H10 HA mutants with human and avian receptors analogs, receptor binding studies, and tissue staining experiments illustrate the important role of the 150-loop in H10 receptor specificity.</p>
</abstract>
<abstract abstract-type="graphical" id="Abs2"><title>Graphical abstract</title>
<p id="P2"><graphic xlink:href="nihms864988u1.jpg" position="anchor" orientation="portrait"></graphic>
</p>
</abstract>
</article-meta>
</front>
</pmc>
</record>
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