From Variation of Influenza Viral Proteins to Vaccine Development
Identifieur interne : 000D78 ( Pmc/Curation ); précédent : 000D77; suivant : 000D79From Variation of Influenza Viral Proteins to Vaccine Development
Auteurs : Wandi Zhu ; Chao Wang ; Bao-Zhong WangSource :
- International Journal of Molecular Sciences [ 1422-0067 ] ; 2017.
Abstract
Recurrent influenza epidemics and occasional pandemics are one of the most important global public health concerns and are major causes of human morbidity and mortality. Influenza viruses can evolve through antigen drift and shift to overcome the barriers of human immunity, leading to host adaption and transmission. Mechanisms underlying this viral evolution are gradually being elucidated. Vaccination is an effective method for the prevention of influenza virus infection. However, the emergence of novel viruses, including the 2009 pandemic influenza A (H1N1), the avian influenza A virus (H7N9), and the highly pathogenic avian influenza A virus (HPAI H5N1), that have infected human populations frequently in recent years reveals the tremendous challenges to the current influenza vaccine strategy. A better vaccine that provides protection against a wide spectrum of various influenza viruses and long-lasting immunity is urgently required. Here, we review the evolutionary changes of several important influenza proteins and the influence of these changes on viral antigenicity, host adaption, and viral pathogenicity. Furthermore, we discuss the development of a potent universal influenza vaccine based on this knowledge.
Url:
DOI: 10.3390/ijms18071554
PubMed: 28718801
PubMed Central: 5536042
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">From Variation of Influenza Viral Proteins to Vaccine Development</title><author><name sortKey="Zhu, Wandi" sort="Zhu, Wandi" uniqKey="Zhu W" first="Wandi" last="Zhu">Wandi Zhu</name></author><author><name sortKey="Wang, Chao" sort="Wang, Chao" uniqKey="Wang C" first="Chao" last="Wang">Chao Wang</name></author><author><name sortKey="Wang, Bao Zhong" sort="Wang, Bao Zhong" uniqKey="Wang B" first="Bao-Zhong" last="Wang">Bao-Zhong Wang</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">28718801</idno><idno type="pmc">5536042</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5536042</idno><idno type="RBID">PMC:5536042</idno><idno type="doi">10.3390/ijms18071554</idno><date when="2017">2017</date><idno type="wicri:Area/Pmc/Corpus">000D78</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000D78</idno><idno type="wicri:Area/Pmc/Curation">000D78</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000D78</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">From Variation of Influenza Viral Proteins to Vaccine Development</title><author><name sortKey="Zhu, Wandi" sort="Zhu, Wandi" uniqKey="Zhu W" first="Wandi" last="Zhu">Wandi Zhu</name></author><author><name sortKey="Wang, Chao" sort="Wang, Chao" uniqKey="Wang C" first="Chao" last="Wang">Chao Wang</name></author><author><name sortKey="Wang, Bao Zhong" sort="Wang, Bao Zhong" uniqKey="Wang B" first="Bao-Zhong" last="Wang">Bao-Zhong Wang</name></author></analytic><series><title level="j">International Journal of Molecular Sciences</title><idno type="eISSN">1422-0067</idno><imprint><date when="2017">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Recurrent influenza epidemics and occasional pandemics are one of the most important global public health concerns and are major causes of human morbidity and mortality. Influenza viruses can evolve through antigen drift and shift to overcome the barriers of human immunity, leading to host adaption and transmission. Mechanisms underlying this viral evolution are gradually being elucidated. Vaccination is an effective method for the prevention of influenza virus infection. However, the emergence of novel viruses, including the 2009 pandemic influenza A (H1N1), the avian influenza A virus (H7N9), and the highly pathogenic avian influenza A virus (HPAI H5N1), that have infected human populations frequently in recent years reveals the tremendous challenges to the current influenza vaccine strategy. A better vaccine that provides protection against a wide spectrum of various influenza viruses and long-lasting immunity is urgently required. Here, we review the evolutionary changes of several important influenza proteins and the influence of these changes on viral antigenicity, host adaption, and viral pathogenicity. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Int J Mol Sci</journal-id><journal-id journal-id-type="iso-abbrev">Int J Mol Sci</journal-id><journal-id journal-id-type="publisher-id">ijms</journal-id><journal-title-group><journal-title>International Journal of Molecular Sciences</journal-title></journal-title-group><issn pub-type="epub">1422-0067</issn><publisher><publisher-name>MDPI</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">28718801</article-id><article-id pub-id-type="pmc">5536042</article-id><article-id pub-id-type="doi">10.3390/ijms18071554</article-id><article-id pub-id-type="publisher-id">ijms-18-01554</article-id><article-categories><subj-group subj-group-type="heading"><subject>Review</subject></subj-group></article-categories><title-group><article-title>From Variation of Influenza Viral Proteins to Vaccine Development</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Zhu</surname><given-names>Wandi</given-names></name></contrib><contrib contrib-type="author"><name><surname>Wang</surname><given-names>Chao</given-names></name></contrib><contrib contrib-type="author"><contrib-id contrib-id-type="orcid" authenticated="true">https://orcid.org/0000-0002-1561-4318</contrib-id><name><surname>Wang</surname><given-names>Bao-Zhong</given-names></name><xref rid="c1-ijms-18-01554" ref-type="corresp">*</xref></contrib></contrib-group><aff id="af1-ijms-18-01554">Center for Inflammation, Immunity & Infection, Georgia State University Institute for Biomedical Sciences, Atlanta, GA 30303, USA;<email>wzhu3@gsu.edu</email> (W.Z.);<email>cwang45@gsu.edu</email> (C.W.)</aff><author-notes><corresp id="c1-ijms-18-01554"><label>*</label>Correspondence: <email>bwang23@gsu.edu</email>; Tel.: +1-404-413-3652</corresp></author-notes><pub-date pub-type="epub"><day>18</day><month>7</month><year>2017</year></pub-date><pub-date pub-type="collection"><month>7</month><year>2017</year></pub-date><volume>18</volume><issue>7</issue><elocation-id>1554</elocation-id><history><date date-type="received"><day>20</day><month>6</month><year>2017</year></date><date date-type="accepted"><day>14</day><month>7</month><year>2017</year></date></history><permissions><copyright-statement>© 2017 by the authors.</copyright-statement><copyright-year>2017</copyright-year><license license-type="open-access"><license-p>Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (<ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by/4.0/">http://creativecommons.org/licenses/by/4.0/</ext-link>).</license-p></license></permissions><abstract><p>Recurrent influenza epidemics and occasional pandemics are one of the most important global public health concerns and are major causes of human morbidity and mortality. Influenza viruses can evolve through antigen drift and shift to overcome the barriers of human immunity, leading to host adaption and transmission. Mechanisms underlying this viral evolution are gradually being elucidated. Vaccination is an effective method for the prevention of influenza virus infection. However, the emergence of novel viruses, including the 2009 pandemic influenza A (H1N1), the avian influenza A virus (H7N9), and the highly pathogenic avian influenza A virus (HPAI H5N1), that have infected human populations frequently in recent years reveals the tremendous challenges to the current influenza vaccine strategy. A better vaccine that provides protection against a wide spectrum of various influenza viruses and long-lasting immunity is urgently required. Here, we review the evolutionary changes of several important influenza proteins and the influence of these changes on viral antigenicity, host adaption, and viral pathogenicity. Furthermore, we discuss the development of a potent universal influenza vaccine based on this knowledge.</p></abstract><kwd-group><kwd>influenza virus</kwd><kwd>antigenic drift and shift</kwd><kwd>universal influenza vaccine</kwd></kwd-group></article-meta></front><floats-group><fig id="ijms-18-01554-f001" orientation="portrait" position="float"><label>Figure 1</label><caption><p>Influenza virus particle and life cycle. Influenza viral proteins participating in different steps of virus infection are indicated. HA, hemagglutinin; NA, neuraminidase; M1, matrix 1 protein; M2, matrix 2 protein; NP, nucleoprotein; PB2, polymerase basic protein 2; PB1, polymerase basic protein 1; PA, polymerase acidic protein; NS1, nonstructural protein 1; NS2, nuclear export protein.</p></caption><graphic xlink:href="ijms-18-01554-g001"></graphic></fig><table-wrap id="ijms-18-01554-t001" orientation="portrait" position="float"><object-id pub-id-type="pii">ijms-18-01554-t001_Table 1</object-id><label>Table 1</label><caption><p>Summary of critical mutation sites for the function of influenza viral proteins.</p></caption><table frame="hsides" rules="groups"><thead><tr><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Influenza Viral Protein</th><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Functions</th><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Mutation Sites</th><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Conservation Sites</th><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Applications in Vaccines</th></tr></thead><tbody><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Hemagglutinin (HA)</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Receptor binding, Membrane fusion</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Receptor binding site, Glycosylation site, Proteolytic cleavage site</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Stalk domain</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">HA stalk based vaccines, HA head COBRAs * Live attenuated vaccine strains</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Neuraminidase (NA)</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Virus releasing, Prevention aggregation, Penetration through mucus layer</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Deletion in stalk domain, Glycosylation in stalk domain, Surface loops surrounding the enzyme active site</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Enzymatic active site</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Induction of NA immunity, Conserved epitopes in enzymatic site</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Matrix 2 (M2)</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Ion channel protein, Viral uncoating, Maintaining HA configuration, Virion budding and scission</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Amantadine-resistant mutations V27A, S31N, and L26F</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Ectodomain, An amphipathic helix in cytoplasmic tail</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">M2e ectodomain based vaccines</td></tr><tr><td rowspan="4" align="center" valign="middle" style="border-bottom:solid thin" colspan="1">Viral ribonucleoprotein complex (vRNP)</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">NP-single strand RNA binding protein</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">NP-309K, 50G Temperature sensitive mutations</td><td rowspan="4" align="center" valign="middle" style="border-bottom:solid thin" colspan="1"></td><td rowspan="4" align="center" valign="middle" style="border-bottom:solid thin" colspan="1">Live attenuated vaccine strains Conserved peptides in NP, PA and PB</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">PB1-RNA dependent RNA polymerase</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">PB1-105S</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">PB2-binding host mRNA caps</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">PB2-627K, 701N, 591K</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">PA-essential for polymerase function</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">PA-552S, 224P, 383D</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Nonstructural 1 protein (NS1)</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">RNA binding, Type I interferon antagonism, Enhancing viral RNA translation, Inhibition of host mRNA processing</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">NS1-S42P, D92E, V149A NS1-103L, 106I</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1"></td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Live attenuated vaccine strains</td></tr></tbody></table><table-wrap-foot><fn><p>* COBRA: Computationally optimized broadly reactive antigen.</p></fn></table-wrap-foot></table-wrap></floats-group></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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