Structural Insights for Anti-Influenza Vaccine Design
Identifieur interne : 000D17 ( Pmc/Curation ); précédent : 000D16; suivant : 000D18Structural Insights for Anti-Influenza Vaccine Design
Auteurs : Lifen Han [République populaire de Chine] ; Cong Chen [République populaire de Chine] ; Xianlin Han [République populaire de Chine] ; Shujin Lin [République populaire de Chine] ; Xiulan Ao [République populaire de Chine] ; Xiao Han [République populaire de Chine] ; Jianmin Wang [République populaire de Chine] ; Hanhui Ye [République populaire de Chine]Source :
- Computational and Structural Biotechnology Journal [ 2001-0370 ] ; 2019.
Abstract
Influenza A virus are a persistent and significant threat to human health, and current vaccines do not provide sufficient protection due to antigenic drift, which allows influenza viruses to easily escape immune surveillance and antiviral drug activity. Influenza hemagglutinin (HA) is a glycoprotein needed for the entry of enveloped influenza viruses into host cells and is a potential target for anti-influenza humoral immune responses. In recent years, a number of broadly neutralizing antibodies (bnAbs) have been isolated, and their relative structural information obtained from the crystallization of influenza antigens in complex with bnAbs has provided some new insights into future influenza vaccine research. Here, we review the current knowledge of the HA-targeted bnAbs and the structure-based mechanisms contributing to neutralization. We also discuss the potential for this structure-based approach to overcome the challenge of obtaining a highly desired “universal” influenza vaccine, especially on small proteins and peptides.
Url:
DOI: 10.1016/j.csbj.2019.03.009
PubMed: 31007873
PubMed Central: 6458449
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last="Chen">Cong Chen</name><affiliation wicri:level="1"><nlm:aff id="af0015">NHC Key Laboratory of Systems Biology of Pathogens, Institute of Pathogen Biology, Chinese Academy of Medical Sciences & Peking Union Medical College, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>NHC Key Laboratory of Systems Biology of Pathogens, Institute of Pathogen Biology, Chinese Academy of Medical Sciences & Peking Union Medical College</wicri:regionArea></affiliation></author><author><name sortKey="Han, Xianlin" sort="Han, Xianlin" uniqKey="Han X" first="Xianlin" last="Han">Xianlin Han</name><affiliation wicri:level="1"><nlm:aff id="af0020">Department of General Surgery, Peking Union Medical College Hospital, Beijing, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Department of General Surgery, Peking Union Medical College Hospital, Beijing</wicri:regionArea></affiliation></author><author><name sortKey="Lin, Shujin" sort="Lin, Shujin" uniqKey="Lin S" first="Shujin" last="Lin">Shujin Lin</name><affiliation wicri:level="1"><nlm:aff id="af0005">The United Innovation of Mengchao Hepatobiliary Technology Key Laboratory of Fujian Province, Mengchao Hepatobiliary Hospital of Fujian Medical University, Fuzhou 350025, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>The United Innovation of Mengchao Hepatobiliary Technology Key Laboratory of Fujian Province, Mengchao Hepatobiliary Hospital of Fujian Medical University, Fuzhou 350025</wicri:regionArea></affiliation></author><author><name sortKey="Ao, Xiulan" sort="Ao, Xiulan" uniqKey="Ao X" first="Xiulan" last="Ao">Xiulan Ao</name><affiliation wicri:level="1"><nlm:aff id="af0005">The United Innovation of Mengchao Hepatobiliary Technology Key Laboratory of Fujian Province, Mengchao Hepatobiliary Hospital of Fujian Medical University, Fuzhou 350025, China</nlm:aff><country 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Academy of Medical Sciences & Peking Union Medical College, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>NHC Key Laboratory of Systems Biology of Pathogens, Institute of Pathogen Biology, Chinese Academy of Medical Sciences & Peking Union Medical College</wicri:regionArea></affiliation></author><author><name sortKey="Ye, Hanhui" sort="Ye, Hanhui" uniqKey="Ye H" first="Hanhui" last="Ye">Hanhui Ye</name><affiliation wicri:level="1"><nlm:aff id="af0005">The United Innovation of Mengchao Hepatobiliary Technology Key Laboratory of Fujian Province, Mengchao Hepatobiliary Hospital of Fujian Medical University, Fuzhou 350025, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>The United Innovation of Mengchao Hepatobiliary Technology Key Laboratory of Fujian Province, Mengchao Hepatobiliary Hospital of Fujian Medical University, Fuzhou 350025</wicri:regionArea></affiliation></author></analytic><series><title level="j">Computational and Structural Biotechnology Journal</title><idno type="eISSN">2001-0370</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>Influenza A virus are a persistent and significant threat to human health, and current vaccines do not provide sufficient protection due to antigenic drift, which allows influenza viruses to easily escape immune surveillance and antiviral drug activity. Influenza hemagglutinin (HA) is a glycoprotein needed for the entry of enveloped influenza viruses into host cells and is a potential target for anti-influenza humoral immune responses. In recent years, a number of broadly neutralizing antibodies (bnAbs) have been isolated, and their relative structural information obtained from the crystallization of influenza antigens in complex with bnAbs has provided some new insights into future influenza vaccine research. Here, we review the current knowledge of the HA-targeted bnAbs and the structure-based mechanisms contributing to neutralization. We also discuss the potential for this structure-based approach to overcome the challenge of obtaining a highly desired “universal” influenza vaccine, especially on small proteins and peptides.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct><analytic><author><name sortKey="Alarcon, C R" uniqKey="Alarcon C">C.R. Alarcon</name></author><author><name sortKey="Goodarzi, H" uniqKey="Goodarzi H">H. Goodarzi</name></author><author><name sortKey="Lee, H" uniqKey="Lee H">H. Lee</name></author><author><name sortKey="Liu, X" uniqKey="Liu X">X. Liu</name></author><author><name sortKey="Tavazoie, S" uniqKey="Tavazoie S">S. Tavazoie</name></author><author><name sortKey="Tavazoie, S F" uniqKey="Tavazoie S">S.F. Tavazoie</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Andrews, S F" uniqKey="Andrews S">S.F. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Comput Struct Biotechnol J</journal-id><journal-id journal-id-type="iso-abbrev">Comput Struct Biotechnol J</journal-id><journal-title-group><journal-title>Computational and Structural Biotechnology Journal</journal-title></journal-title-group><issn pub-type="epub">2001-0370</issn><publisher><publisher-name>Research Network of Computational and Structural Biotechnology</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">31007873</article-id><article-id pub-id-type="pmc">6458449</article-id><article-id pub-id-type="publisher-id">S2001-0370(18)30305-2</article-id><article-id pub-id-type="doi">10.1016/j.csbj.2019.03.009</article-id><article-categories><subj-group subj-group-type="heading"><subject>Review Article</subject></subj-group></article-categories><title-group><article-title>Structural Insights for Anti-Influenza Vaccine Design</article-title></title-group><contrib-group><contrib contrib-type="author" id="au0005"><name><surname>Han</surname><given-names>Lifen</given-names></name><xref rid="af0005" ref-type="aff">a</xref><xref rid="af0010" ref-type="aff">b</xref><xref rid="fn0005" ref-type="fn">1</xref></contrib><contrib contrib-type="author" id="au0010"><name><surname>Chen</surname><given-names>Cong</given-names></name><xref rid="af0015" ref-type="aff">c</xref><xref rid="fn0005" ref-type="fn">1</xref></contrib><contrib contrib-type="author" id="au0015"><name><surname>Han</surname><given-names>Xianlin</given-names></name><xref rid="af0020" ref-type="aff">d</xref><xref rid="fn0005" ref-type="fn">1</xref></contrib><contrib contrib-type="author" id="au0020"><name><surname>Lin</surname><given-names>Shujin</given-names></name><xref rid="af0005" ref-type="aff">a</xref><xref rid="fn0005" ref-type="fn">1</xref></contrib><contrib contrib-type="author" id="au0025"><name><surname>Ao</surname><given-names>Xiulan</given-names></name><xref rid="af0005" ref-type="aff">a</xref></contrib><contrib contrib-type="author" id="au0030"><name><surname>Han</surname><given-names>Xiao</given-names></name><email>hanxiao@caas.cn</email><xref rid="af0010" ref-type="aff">b</xref><xref rid="cr0005" ref-type="corresp">⁎</xref></contrib><contrib contrib-type="author" id="au0035"><name><surname>Wang</surname><given-names>Jianmin</given-names></name><email>wangjm8605@163.com</email><xref rid="af0015" ref-type="aff">c</xref><xref rid="cr0005" ref-type="corresp">⁎</xref></contrib><contrib contrib-type="author" id="au0040"><name><surname>Ye</surname><given-names>Hanhui</given-names></name><email>yehanhui@163.com</email><xref rid="af0005" ref-type="aff">a</xref><xref rid="cr0005" ref-type="corresp">⁎</xref></contrib></contrib-group><aff id="af0005"><label>a</label>The United Innovation of Mengchao Hepatobiliary Technology Key Laboratory of Fujian Province, Mengchao Hepatobiliary Hospital of Fujian Medical University, Fuzhou 350025, China</aff><aff id="af0010"><label>b</label>College of Biological Science and Engineering, Fuzhou University, Fuzhou 350108, China</aff><aff id="af0015"><label>c</label>NHC Key Laboratory of Systems Biology of Pathogens, Institute of Pathogen Biology, Chinese Academy of Medical Sciences & Peking Union Medical College, China</aff><aff id="af0020"><label>d</label>Department of General Surgery, Peking Union Medical College Hospital, Beijing, China</aff><author-notes><corresp id="cr0005"><label>⁎</label>Corresponding authors. <email>hanxiao@caas.cn</email><email>wangjm8605@163.com</email><email>yehanhui@163.com</email></corresp><fn id="fn0005"><label>1</label><p id="np0005">These authors contributed equally to this work.</p></fn></author-notes><pub-date pub-type="pmc-release"><day>23</day><month>3</month><year>2019</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on .</pmc-comment>
<pub-date pub-type="collection"><year>2019</year></pub-date><pub-date pub-type="epub"><day>23</day><month>3</month><year>2019</year></pub-date><volume>17</volume><fpage>475</fpage><lpage>483</lpage><history><date date-type="received"><day>27</day><month>11</month><year>2018</year></date><date date-type="rev-recd"><day>17</day><month>3</month><year>2019</year></date><date date-type="accepted"><day>21</day><month>3</month><year>2019</year></date></history><permissions><copyright-statement>© 2019 The Authors. Published by Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology.</copyright-statement><copyright-year>2019</copyright-year><copyright-holder></copyright-holder><license license-type="CC BY" xlink:href="http://creativecommons.org/licenses/by/4.0/"><license-p>This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).</license-p></license></permissions><abstract id="ab0005"><p>Influenza A virus are a persistent and significant threat to human health, and current vaccines do not provide sufficient protection due to antigenic drift, which allows influenza viruses to easily escape immune surveillance and antiviral drug activity. Influenza hemagglutinin (HA) is a glycoprotein needed for the entry of enveloped influenza viruses into host cells and is a potential target for anti-influenza humoral immune responses. In recent years, a number of broadly neutralizing antibodies (bnAbs) have been isolated, and their relative structural information obtained from the crystallization of influenza antigens in complex with bnAbs has provided some new insights into future influenza vaccine research. Here, we review the current knowledge of the HA-targeted bnAbs and the structure-based mechanisms contributing to neutralization. We also discuss the potential for this structure-based approach to overcome the challenge of obtaining a highly desired “universal” influenza vaccine, especially on small proteins and peptides.</p></abstract><abstract abstract-type="graphical" id="ab0010"><title>Graphical abstract</title><p><fig id="f0025" position="anchor"><alt-text id="al0035">Unlabelled Image</alt-text><graphic xlink:href="ga1"></graphic></fig></p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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