A Single Amino Acid Substitution at Residue 218 of Hemagglutinin Improves the Growth of Influenza A(H7N9) Candidate Vaccine Viruses
Identifieur interne : 000B54 ( Pmc/Curation ); précédent : 000B53; suivant : 000B55A Single Amino Acid Substitution at Residue 218 of Hemagglutinin Improves the Growth of Influenza A(H7N9) Candidate Vaccine Viruses
Auteurs : Xing Li [États-Unis] ; Yamei Gao [États-Unis] ; Zhiping Ye [États-Unis]Source :
- Journal of Virology [ 0022-538X ] ; 2019.
Abstract
The circulating avian influenza A(H7N9) has caused recurrent epidemic waves with high mortality in China since 2013, in which the alarming fifth wave crossing 2016 and 2017 was highlighted by a large number of human infections and the emergence of highly pathogenic avian influenza (HPAI) A(H7N9) strains in human cases. We generated low-pathogenic reassortant CVVs derived from the emerging A(H7N9) with improved virus replication and protein yield in both MDCK cells and eggs by introducing a single substitution, G218E, into HA, which was associated with reducing HA receptor binding and subsequently balancing HA-NA functions. The
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DOI: 10.1128/JVI.00570-19
PubMed: 31270231
PubMed Central: 6744242
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">A Single Amino Acid Substitution at Residue 218 of Hemagglutinin Improves the Growth of Influenza A(H7N9) Candidate Vaccine Viruses</title><author><name sortKey="Li, Xing" sort="Li, Xing" uniqKey="Li X" first="Xing" last="Li">Xing Li</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Division of Viral Products, Center for Biologics Evaluation and Research, Silver Spring, Maryland, USA</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Division of Viral Products, Center for Biologics Evaluation and Research, Silver Spring, Maryland</wicri:regionArea></affiliation></author><author><name sortKey="Gao, Yamei" sort="Gao, Yamei" uniqKey="Gao Y" first="Yamei" last="Gao">Yamei Gao</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Division of Viral Products, Center for Biologics Evaluation and Research, Silver Spring, Maryland, USA</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Division of Viral Products, Center for Biologics Evaluation and Research, Silver Spring, Maryland</wicri:regionArea></affiliation></author><author><name sortKey="Ye, Zhiping" sort="Ye, Zhiping" uniqKey="Ye Z" first="Zhiping" last="Ye">Zhiping Ye</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Division of Viral Products, Center for Biologics Evaluation and Research, Silver Spring, Maryland, USA</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Division of Viral Products, Center for Biologics Evaluation and Research, Silver Spring, Maryland</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">31270231</idno><idno type="pmc">6744242</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6744242</idno><idno type="RBID">PMC:6744242</idno><idno type="doi">10.1128/JVI.00570-19</idno><date when="2019">2019</date><idno type="wicri:Area/Pmc/Corpus">000B54</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000B54</idno><idno type="wicri:Area/Pmc/Curation">000B54</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000B54</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">A Single Amino Acid Substitution at Residue 218 of Hemagglutinin Improves the Growth of Influenza A(H7N9) Candidate Vaccine Viruses</title><author><name sortKey="Li, Xing" sort="Li, Xing" uniqKey="Li X" first="Xing" last="Li">Xing Li</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Division of Viral Products, Center for Biologics Evaluation and Research, Silver Spring, Maryland, USA</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Division of Viral Products, Center for Biologics Evaluation and Research, Silver Spring, Maryland</wicri:regionArea></affiliation></author><author><name sortKey="Gao, Yamei" sort="Gao, Yamei" uniqKey="Gao Y" first="Yamei" last="Gao">Yamei Gao</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Division of Viral Products, Center for Biologics Evaluation and Research, Silver Spring, Maryland, USA</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Division of Viral Products, Center for Biologics Evaluation and Research, Silver Spring, Maryland</wicri:regionArea></affiliation></author><author><name sortKey="Ye, Zhiping" sort="Ye, Zhiping" uniqKey="Ye Z" first="Zhiping" last="Ye">Zhiping Ye</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Division of Viral Products, Center for Biologics Evaluation and Research, Silver Spring, Maryland, USA</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Division of Viral Products, Center for Biologics Evaluation and Research, Silver Spring, Maryland</wicri:regionArea></affiliation></author></analytic><series><title level="j">Journal of Virology</title><idno type="ISSN">0022-538X</idno><idno type="eISSN">1098-5514</idno><imprint><date when="2019">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The circulating avian influenza A(H7N9) has caused recurrent epidemic waves with high mortality in China since 2013, in which the alarming fifth wave crossing 2016 and 2017 was highlighted by a large number of human infections and the emergence of highly pathogenic avian influenza (HPAI) A(H7N9) strains in human cases. We generated low-pathogenic reassortant CVVs derived from the emerging A(H7N9) with improved virus replication and protein yield in both MDCK cells and eggs by introducing a single substitution, G218E, into HA, which was associated with reducing HA receptor binding and subsequently balancing HA-NA functions. The <italic>in vitro</italic> and <italic>in vivo</italic> experiments demonstrated comparable antigenicity of the G218E CVVs with that of their wild-type (WT) counterparts, and both the WT and the G218E CVVs fully protected ferrets from parental HPAI virus challenge. 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<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><journal-title-group><journal-title>Journal of Virology</journal-title></journal-title-group><issn pub-type="ppub">0022-538X</issn><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></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">31270231</article-id><article-id pub-id-type="pmc">6744242</article-id><article-id pub-id-type="publisher-id">00570-19</article-id><article-id pub-id-type="doi">10.1128/JVI.00570-19</article-id><article-categories><subj-group subj-group-type="heading"><subject>Vaccines and Antiviral Agents</subject></subj-group></article-categories><title-group><article-title>A Single Amino Acid Substitution at Residue 218 of Hemagglutinin Improves the Growth of Influenza A(H7N9) Candidate Vaccine Viruses</article-title><alt-title alt-title-type="running-head">G218E Substitution in HA and Improved H7N9 CVV Growth</alt-title><alt-title alt-title-type="short-authors">Li et al.</alt-title></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><name><surname>Li</surname><given-names>Xing</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref></contrib><contrib contrib-type="author"><name><surname>Gao</surname><given-names>Yamei</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref></contrib><contrib contrib-type="author" corresp="yes"><name><surname>Ye</surname><given-names>Zhiping</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref></contrib><aff id="aff1"><label>a</label><addr-line>Division of Viral Products, Center for Biologics Evaluation and Research, Silver Spring, Maryland, USA</addr-line></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 Xing Li, <email>xing.li@fda.hhs.gov</email>, or Zhiping Ye, <email>Zhiping.ye@fda.hhs.gov</email>.</corresp><fn fn-type="other"><p><bold>Citation</bold> Li X, Gao Y, Ye Z. 2019. A single amino acid substitution at residue 218 of hemagglutinin improves the growth of influenza A(H7N9) candidate vaccine viruses. J Virol 93:e00570-19. <ext-link ext-link-type="uri" xlink:href="https://doi.org/10.1128/JVI.00570-19">https://doi.org/10.1128/JVI.00570-19</ext-link>.</p></fn></author-notes><pub-date pub-type="epreprint"><day>3</day><month>7</month><year>2019</year></pub-date><pub-date pub-type="epub"><day>12</day><month>9</month><year>2019</year></pub-date><pub-date pub-type="collection"><day>1</day><month>10</month><year>2019</year></pub-date><pub-date pub-type="pmc-release"><day>12</day><month>9</month><year>2019</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on the
<volume>93</volume><issue>19</issue><elocation-id>e00570-19</elocation-id><history><date date-type="received"><day>4</day><month>4</month><year>2019</year></date><date date-type="accepted"><day>28</day><month>6</month><year>2019</year></date></history><permissions><copyright-statement>Copyright © 2019 Li et al.</copyright-statement><copyright-year>2019</copyright-year><copyright-holder>Li et al.</copyright-holder><license license-type="open-access" xlink:href="https://creativecommons.org/licenses/by/4.0/"><license-p>This is an open-access article distributed under the terms of the <ext-link ext-link-type="uri" xlink:href="https://creativecommons.org/licenses/by/4.0/">Creative Commons Attribution 4.0 International license</ext-link>.</license-p></license></permissions><self-uri content-type="pdf" xlink:href="JVI.00570-19.pdf"></self-uri><abstract abstract-type="precis"><p>The circulating avian influenza A(H7N9) has caused recurrent epidemic waves with high mortality in China since 2013, in which the alarming fifth wave crossing 2016 and 2017 was highlighted by a large number of human infections and the emergence of highly pathogenic avian influenza (HPAI) A(H7N9) strains in human cases. We generated low-pathogenic reassortant CVVs derived from the emerging A(H7N9) with improved virus replication and protein yield in both MDCK cells and eggs by introducing a single substitution, G218E, into HA, which was associated with reducing HA receptor binding and subsequently balancing HA-NA functions. The <italic>in vitro</italic> and <italic>in vivo</italic> experiments demonstrated comparable antigenicity of the G218E CVVs with that of their wild-type (WT) counterparts, and both the WT and the G218E CVVs fully protected ferrets from parental HPAI virus challenge. With high yield traits and the anticipated antigenicity, the G218E CVVs should benefit preparedness against the threat of an A(H7N9) influenza pandemic.</p></abstract><abstract><title>ABSTRACT</title><p>The potential avian influenza pandemic remains a threat to public health, as the avian-origin influenza A(H7N9) virus has caused more than 1,560 laboratory-confirmed human infections since 2013, with nearly 40% mortality. Development of low-pathogenic candidate vaccine viruses (CVVs) for vaccine production is essential for pandemic preparedness. However, the suboptimal growth of CVVs in mammalian cells and chicken eggs is often a challenge. By introducing a single adaptive substitution, G218E, into the hemagglutinin (HA), we generated reassortant A(H7N9)-G218E CVVs that were characterized by significantly enhanced growth in both cells and eggs. These G218E CVVs retained the original antigenicity, as determined by a hemagglutination inhibition assay, and effectively protected ferrets from lethal challenge with the highly pathogenic parental virus. We found that the suboptimal replication of the parental H7 CVVs was associated with impeded progeny virus release as a result of strong HA receptor binding relative to weak neuraminidase (NA) cleavage of receptors. In contrast, the G218E-mediated growth improvement was attributed to relatively balanced HA and NA functions, resulted from reduced HA binding to both human- and avian-type receptors, and thus facilitated NA-mediated virus release. Our findings revealed that a single amino acid mutation at residue 218 of the HA improved the growth of A(H7N9) influenza virus by balancing HA and NA functions, shedding light on an alternative approach for optimizing certain influenza CVVs.</p><p><bold>IMPORTANCE</bold> The circulating avian influenza A(H7N9) has caused recurrent epidemic waves with high mortality in China since 2013, in which the alarming fifth wave crossing 2016 and 2017 was highlighted by a large number of human infections and the emergence of highly pathogenic avian influenza (HPAI) A(H7N9) strains in human cases. We generated low-pathogenic reassortant CVVs derived from the emerging A(H7N9) with improved virus replication and protein yield in both MDCK cells and eggs by introducing a single substitution, G218E, into HA, which was associated with reducing HA receptor binding and subsequently balancing HA-NA functions. The <italic>in vitro</italic> and <italic>in vivo</italic> experiments demonstrated comparable antigenicity of the G218E CVVs with that of their wild-type (WT) counterparts, and both the WT and the G218E CVVs fully protected ferrets from parental HPAI virus challenge. With high yield traits and the anticipated antigenicity, the G218E CVVs should benefit preparedness against the threat of an A(H7N9) influenza pandemic.</p></abstract><kwd-group><title>KEYWORDS</title><kwd>influenza A(H7N9) virus</kwd><kwd>balancing HA and NA functions</kwd><kwd>pandemic preparedness</kwd><kwd>pathogenesis in ferret</kwd><kwd>vaccine protein yield</kwd><kwd>virus replication</kwd></kwd-group><counts><fig-count count="5"></fig-count><table-count count="2"></table-count><equation-count count="1"></equation-count><ref-count count="47"></ref-count><page-count count="15"></page-count><word-count count="10165"></word-count></counts><custom-meta-group><custom-meta><meta-name>cover-date</meta-name><meta-value>October 2019</meta-value></custom-meta></custom-meta-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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