The epitope regions of H1-subtype influenza A, with application to vaccine efficacy
Identifieur interne : 000C24 ( Pmc/Curation ); précédent : 000C23; suivant : 000C25The epitope regions of H1-subtype influenza A, with application to vaccine efficacy
Auteurs : Michael W. Deem [États-Unis] ; Keyao PanSource :
- Protein Engineering, Design and Selection [ 1741-0126 ] ; 2009.
Abstract
The recent emergence of H1N1 (swine flu) illustrates the ability of the influenza virus to create antigens new to the human immune system, even within a given hemagglutinin and neuraminidase subtype. This new H1N1 strain is sufficiently distinct, for example, from the A/Brisbane/59/2007 (H1N1)-like virus strain of influenza in the 2008/09 Northern hemisphere vaccine that protection is not expected to be substantial. The human immune system responds primarily to the five epitope regions of the hemagglutinin protein. By determining the fraction of amino acids that differ between a vaccine strain and a viral challenge strain in the dominant epitope regions, a measure of antigenic distance that correlates with epidemiological studies of H3 influenza A vaccine efficacy in humans with
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DOI: 10.1093/protein/gzp027
PubMed: 19578121
PubMed Central: 3307478
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The epitope regions of H1-subtype influenza A, with application to vaccine efficacy</title><author><name sortKey="Deem, Michael W" sort="Deem, Michael W" uniqKey="Deem M" first="Michael W." last="Deem">Michael W. Deem</name><affiliation><nlm:aff wicri:cut=" and" id="af1"><addr-line>Departments of Bioengineering</addr-line></nlm:aff></affiliation><affiliation wicri:level="1"><nlm:aff id="af2"><addr-line>Physics and Astronomy</addr-line>,<institution>Rice University</institution>,<addr-line>6100 Main Street, MS 142, Houston, TX 77005-1892</addr-line>,<country>USA</country></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Pan, Keyao" sort="Pan, Keyao" uniqKey="Pan K" first="Keyao" last="Pan">Keyao Pan</name><affiliation><nlm:aff wicri:cut=" and" id="af1"><addr-line>Departments of Bioengineering</addr-line></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">19578121</idno><idno type="pmc">3307478</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3307478</idno><idno type="RBID">PMC:3307478</idno><idno type="doi">10.1093/protein/gzp027</idno><date when="2009">2009</date><idno type="wicri:Area/Pmc/Corpus">000C24</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000C24</idno><idno type="wicri:Area/Pmc/Curation">000C24</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000C24</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">The epitope regions of H1-subtype influenza A, with application to vaccine efficacy</title><author><name sortKey="Deem, Michael W" sort="Deem, Michael W" uniqKey="Deem M" first="Michael W." last="Deem">Michael W. Deem</name><affiliation><nlm:aff wicri:cut=" and" id="af1"><addr-line>Departments of Bioengineering</addr-line></nlm:aff></affiliation><affiliation wicri:level="1"><nlm:aff id="af2"><addr-line>Physics and Astronomy</addr-line>,<institution>Rice University</institution>,<addr-line>6100 Main Street, MS 142, Houston, TX 77005-1892</addr-line>,<country>USA</country></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Pan, Keyao" sort="Pan, Keyao" uniqKey="Pan K" first="Keyao" last="Pan">Keyao Pan</name><affiliation><nlm:aff wicri:cut=" and" id="af1"><addr-line>Departments of Bioengineering</addr-line></nlm:aff></affiliation></author></analytic><series><title level="j">Protein Engineering, Design and Selection</title><idno type="ISSN">1741-0126</idno><idno type="eISSN">1741-0134</idno><imprint><date when="2009">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The recent emergence of H1N1 (swine flu) illustrates the ability of the influenza virus to create antigens new to the human immune system, even within a given hemagglutinin and neuraminidase subtype. This new H1N1 strain is sufficiently distinct, for example, from the A/Brisbane/59/2007 (H1N1)-like virus strain of influenza in the 2008/09 Northern hemisphere vaccine that protection is not expected to be substantial. The human immune system responds primarily to the five epitope regions of the hemagglutinin protein. By determining the fraction of amino acids that differ between a vaccine strain and a viral challenge strain in the dominant epitope regions, a measure of antigenic distance that correlates with epidemiological studies of H3 influenza A vaccine efficacy in humans with <italic>R</italic><sup>2</sup> = 0.81 is derived. This measure of antigenic distance is called <italic>p</italic><sub>epitope</sub>. The relation between vaccine efficacy and <italic>p</italic><sub>epitope</sub> is given by <italic>E</italic> = 0.47 – 2.47 × <italic>p</italic><sub>epitope</sub>. We here identify the epitope regions of H1 hemagglutinin, so that vaccine efficacy may be reliably estimated for H1N1 influenza A.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Bush, R M" uniqKey="Bush R">R.M. Bush</name></author><author><name sortKey="Fitch, W M" uniqKey="Fitch W">W.M. Fitch</name></author><author><name sortKey="Bender, C A" uniqKey="Bender C">C.A. Bender</name></author><author><name sortKey="Cox, N J" uniqKey="Cox N">N.J. Cox</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Caton, A J" uniqKey="Caton A">A.J. Caton</name></author><author><name sortKey="Brownlee, G G" uniqKey="Brownlee G">G.G. Brownlee</name></author><author><name sortKey="Yewdell, J W" uniqKey="Yewdell J">J.W. Yewdell</name></author><author><name sortKey="Gerhard, W" uniqKey="Gerhard W">W. Gerhard</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Felsenstein, J" uniqKey="Felsenstein J">J. Felsenstein</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Gupta, V" uniqKey="Gupta V">V. Gupta</name></author><author><name sortKey="Earl, D J" uniqKey="Earl D">D.J. Earl</name></author><author><name sortKey="Deem, M W" uniqKey="Deem M">M.W. Deem</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Macken, C" uniqKey="Macken C">C. Macken</name></author><author><name sortKey="Lu, H" uniqKey="Lu H">H. Lu</name></author><author><name sortKey="Goodman, J" uniqKey="Goodman J">J. Goodman</name></author><author><name sortKey="Boykin, L" uniqKey="Boykin L">L. Boykin</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Nakajima, K" uniqKey="Nakajima K">K. Nakajima</name></author><author><name sortKey="Desselberger, U" uniqKey="Desselberger U">U. Desselberger</name></author><author><name sortKey="Palese, P" uniqKey="Palese P">P. Palese</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Nobusawa, E" uniqKey="Nobusawa E">E. Nobusawa</name></author><author><name sortKey="Aoyama, T" uniqKey="Aoyama T">T. Aoyama</name></author><author><name sortKey="Kato, H" uniqKey="Kato H">H. Kato</name></author><author><name sortKey="Suzuki, Y" uniqKey="Suzuki Y">Y. Suzuki</name></author><author><name sortKey="Tateno, Y" uniqKey="Tateno Y">Y. Tateno</name></author><author><name sortKey="Nakajima, K" uniqKey="Nakajima K">K. Nakajima</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Palese, P" uniqKey="Palese P">P. Palese</name></author><author><name sortKey="Tumpey, T M" uniqKey="Tumpey T">T.M. Tumpey</name></author><author><name sortKey="Garcia Sastre, A" uniqKey="Garcia Sastre A">A. Garcia-Sastre</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Smith, D J" uniqKey="Smith D">D.J. Smith</name></author><author><name sortKey="Forrest, S" uniqKey="Forrest S">S. Forrest</name></author><author><name sortKey="Ackley, D H" uniqKey="Ackley D">D.H. Ackley</name></author><author><name sortKey="Perelson, A S" uniqKey="Perelson A">A.S. Perelson</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Smith, D J" uniqKey="Smith D">D.J. Smith</name></author><author><name sortKey="Lapedes, A S" uniqKey="Lapedes A">A.S. Lapedes</name></author><author><name sortKey="De Jong, J C" uniqKey="De Jong J">J.C. de Jong</name></author><author><name sortKey="Bestebroer, T M" uniqKey="Bestebroer T">T.M. Bestebroer</name></author><author><name sortKey="Rimmelzwaan, G F" uniqKey="Rimmelzwaan G">G.F. Rimmelzwaan</name></author><author><name sortKey="Osterhaus, A D M E" uniqKey="Osterhaus A">A.D.M.E. Osterhaus</name></author><author><name sortKey="Fouchier, R A M" uniqKey="Fouchier R">R.A.M. Fouchier</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Winter, G" uniqKey="Winter G">G. Winter</name></author><author><name sortKey="Fields, S" uniqKey="Fields S">S. Fields</name></author><author><name sortKey="Brownlee, G G" uniqKey="Brownlee G">G.G. Brownlee</name></author></analytic></biblStruct><biblStruct></biblStruct><biblStruct><analytic><author><name sortKey="Zhou, H" uniqKey="Zhou H">H. Zhou</name></author><author><name sortKey="Pophale, R" uniqKey="Pophale R">R. Pophale</name></author><author><name sortKey="Deem, M W" uniqKey="Deem M">M.W. Deem</name></author></analytic></biblStruct></listBibl></div1></back></TEI><pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Protein Eng Des Sel</journal-id><journal-id journal-id-type="publisher-id">proeng</journal-id><journal-id journal-id-type="hwp">proeng</journal-id><journal-title-group><journal-title>Protein Engineering, Design and Selection</journal-title></journal-title-group><issn pub-type="ppub">1741-0126</issn><issn pub-type="epub">1741-0134</issn><publisher><publisher-name>Oxford University Press</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">19578121</article-id><article-id pub-id-type="pmc">3307478</article-id><article-id pub-id-type="doi">10.1093/protein/gzp027</article-id><article-id pub-id-type="publisher-id">gzp027</article-id><article-categories><subj-group subj-group-type="heading"><subject>Original Articles</subject></subj-group></article-categories><title-group><article-title>The epitope regions of H1-subtype influenza A, with application to vaccine efficacy</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Deem</surname><given-names>Michael W.</given-names></name><xref ref-type="aff" rid="af1">1</xref><xref ref-type="aff" rid="af2">2</xref><xref ref-type="corresp" rid="cor1">3</xref></contrib><contrib contrib-type="author"><name><surname>Pan</surname><given-names>Keyao</given-names></name><xref ref-type="aff" rid="af1">1</xref></contrib></contrib-group><aff id="af1"><label>1</label><addr-line>Departments of Bioengineering</addr-line> and</aff><aff id="af2"><label>2</label><addr-line>Physics and Astronomy</addr-line>,<institution>Rice University</institution>,<addr-line>6100 Main Street, MS 142, Houston, TX 77005-1892</addr-line>,<country>USA</country></aff><author-notes><corresp id="cor1"><label>3</label>To whom correspondence should be addressed. E-mail: <email>mwdeem@rice.edu</email></corresp></author-notes><pub-date pub-type="ppub"><month>9</month><year>2009</year></pub-date><pub-date pub-type="epub"><day>3</day><month>7</month><year>2009</year></pub-date><pub-date pub-type="pmc-release"><day>3</day><month>7</month><year>2009</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on the
<volume>22</volume><issue>9</issue><issue-title>Computational Methods Special Issue</issue-title><fpage>543</fpage><lpage>546</lpage><history><date date-type="received"><day>28</day><month>5</month><year>2009</year></date><date date-type="rev-recd"><day>28</day><month>5</month><year>2009</year></date><date date-type="accepted"><day>3</day><month>6</month><year>2009</year></date></history><permissions><copyright-statement>© 2009 The Author(s)</copyright-statement><copyright-year>2009</copyright-year><license license-type="creative-commons" xlink:href="http://creativecommons.org/licenses/by-nc/2.0/uk/"><license-p><pmc-comment>CREATIVE COMMONS</pmc-comment>This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (<ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by-nc/2.0/uk/">http://creativecommons.org/licenses/by-nc/2.0/uk/</ext-link>) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.</license-p></license></permissions><abstract><p>The recent emergence of H1N1 (swine flu) illustrates the ability of the influenza virus to create antigens new to the human immune system, even within a given hemagglutinin and neuraminidase subtype. This new H1N1 strain is sufficiently distinct, for example, from the A/Brisbane/59/2007 (H1N1)-like virus strain of influenza in the 2008/09 Northern hemisphere vaccine that protection is not expected to be substantial. The human immune system responds primarily to the five epitope regions of the hemagglutinin protein. By determining the fraction of amino acids that differ between a vaccine strain and a viral challenge strain in the dominant epitope regions, a measure of antigenic distance that correlates with epidemiological studies of H3 influenza A vaccine efficacy in humans with <italic>R</italic><sup>2</sup> = 0.81 is derived. This measure of antigenic distance is called <italic>p</italic><sub>epitope</sub>. The relation between vaccine efficacy and <italic>p</italic><sub>epitope</sub> is given by <italic>E</italic> = 0.47 – 2.47 × <italic>p</italic><sub>epitope</sub>. We here identify the epitope regions of H1 hemagglutinin, so that vaccine efficacy may be reliably estimated for H1N1 influenza A.</p></abstract><kwd-group><kwd>antibody</kwd><kwd>epitopes</kwd><kwd>influenza A</kwd><kwd>swine flu</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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