Links to Exploration step
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Conserved Neutralizing Epitope at Globular Head of Hemagglutinin in H3N2 Influenza Viruses</title><author><name sortKey="Iba, Yoshitaka" sort="Iba, Yoshitaka" uniqKey="Iba Y" first="Yoshitaka" last="Iba">Yoshitaka Iba</name><affiliation><nlm:aff id="aff1">Institute for Comprehensive Medical Science, Fujita Health University, Toyoake, Aichi, Japan</nlm:aff></affiliation></author><author><name sortKey="Fujii, Yoshifumi" sort="Fujii, Yoshifumi" uniqKey="Fujii Y" first="Yoshifumi" last="Fujii">Yoshifumi Fujii</name><affiliation><nlm:aff id="aff2">RIKEN Systems and Structural Biology Center, Suehiro, Tsurumi, Yokohama, Japan</nlm:aff></affiliation></author><author><name sortKey="Ohshima, Nobuko" sort="Ohshima, Nobuko" uniqKey="Ohshima N" first="Nobuko" last="Ohshima">Nobuko Ohshima</name><affiliation><nlm:aff id="aff1">Institute for Comprehensive Medical Science, Fujita Health University, Toyoake, Aichi, Japan</nlm:aff></affiliation></author><author><name sortKey="Sumida, Tomomi" sort="Sumida, Tomomi" uniqKey="Sumida T" first="Tomomi" last="Sumida">Tomomi Sumida</name><affiliation><nlm:aff id="aff2">RIKEN Systems and Structural Biology Center, Suehiro, Tsurumi, Yokohama, Japan</nlm:aff></affiliation></author><author><name sortKey="Kubota Koketsu, Ritsuko" sort="Kubota Koketsu, Ritsuko" uniqKey="Kubota Koketsu R" first="Ritsuko" last="Kubota-Koketsu">Ritsuko Kubota-Koketsu</name><affiliation><nlm:aff id="aff3">Department of Virology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka, Japan</nlm:aff></affiliation></author><author><name sortKey="Ikeda, Mariko" sort="Ikeda, Mariko" uniqKey="Ikeda M" first="Mariko" last="Ikeda">Mariko Ikeda</name><affiliation><nlm:aff id="aff2">RIKEN Systems and Structural Biology Center, Suehiro, Tsurumi, Yokohama, Japan</nlm:aff></affiliation></author><author><name sortKey="Wakiyama, Motoaki" sort="Wakiyama, Motoaki" uniqKey="Wakiyama M" first="Motoaki" last="Wakiyama">Motoaki Wakiyama</name><affiliation><nlm:aff id="aff2">RIKEN Systems and Structural Biology Center, Suehiro, Tsurumi, Yokohama, Japan</nlm:aff></affiliation></author><author><name sortKey="Shirouzu, Mikako" sort="Shirouzu, Mikako" uniqKey="Shirouzu M" first="Mikako" last="Shirouzu">Mikako Shirouzu</name><affiliation><nlm:aff id="aff2">RIKEN Systems and Structural Biology Center, Suehiro, Tsurumi, Yokohama, Japan</nlm:aff></affiliation></author><author><name sortKey="Okada, Jun" sort="Okada, Jun" uniqKey="Okada J" first="Jun" last="Okada">Jun Okada</name><affiliation><nlm:aff id="aff4">Sales and Marketing Division, Medical and Biological Laboratories Co., Ltd., Nagoya, Aichi, Japan</nlm:aff></affiliation></author><author><name sortKey="Okuno, Yoshinobu" sort="Okuno, Yoshinobu" uniqKey="Okuno Y" first="Yoshinobu" last="Okuno">Yoshinobu Okuno</name><affiliation><nlm:aff id="aff5">Kanonji Institute, The Research Foundation for Microbial Diseases, Osaka University, Kanonji, Kagawa, Japan</nlm:aff></affiliation></author><author><name sortKey="Kurosawa, Yoshikazu" sort="Kurosawa, Yoshikazu" uniqKey="Kurosawa Y" first="Yoshikazu" last="Kurosawa">Yoshikazu Kurosawa</name><affiliation><nlm:aff id="aff1">Institute for Comprehensive Medical Science, Fujita Health University, Toyoake, Aichi, Japan</nlm:aff></affiliation></author><author><name sortKey="Yokoyama, Shigeyuki" sort="Yokoyama, Shigeyuki" uniqKey="Yokoyama S" first="Shigeyuki" last="Yokoyama">Shigeyuki Yokoyama</name><affiliation><nlm:aff id="aff2">RIKEN Systems and Structural Biology Center, Suehiro, Tsurumi, Yokohama, Japan</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">24719430</idno><idno type="pmc">4054433</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4054433</idno><idno type="RBID">PMC:4054433</idno><idno type="doi">10.1128/JVI.00420-14</idno><date when="2014">2014</date><idno type="wicri:Area/Pmc/Corpus">000683</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000683</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Conserved Neutralizing Epitope at Globular Head of Hemagglutinin in H3N2 Influenza Viruses</title><author><name sortKey="Iba, Yoshitaka" sort="Iba, Yoshitaka" uniqKey="Iba Y" first="Yoshitaka" last="Iba">Yoshitaka Iba</name><affiliation><nlm:aff id="aff1">Institute for Comprehensive Medical Science, Fujita Health University, Toyoake, Aichi, Japan</nlm:aff></affiliation></author><author><name sortKey="Fujii, Yoshifumi" sort="Fujii, Yoshifumi" uniqKey="Fujii Y" first="Yoshifumi" last="Fujii">Yoshifumi Fujii</name><affiliation><nlm:aff id="aff2">RIKEN Systems and Structural Biology Center, Suehiro, Tsurumi, Yokohama, Japan</nlm:aff></affiliation></author><author><name sortKey="Ohshima, Nobuko" sort="Ohshima, Nobuko" uniqKey="Ohshima N" first="Nobuko" last="Ohshima">Nobuko Ohshima</name><affiliation><nlm:aff id="aff1">Institute for Comprehensive Medical Science, Fujita Health University, Toyoake, Aichi, Japan</nlm:aff></affiliation></author><author><name sortKey="Sumida, Tomomi" sort="Sumida, Tomomi" uniqKey="Sumida T" first="Tomomi" last="Sumida">Tomomi Sumida</name><affiliation><nlm:aff id="aff2">RIKEN Systems and Structural Biology Center, Suehiro, Tsurumi, Yokohama, Japan</nlm:aff></affiliation></author><author><name sortKey="Kubota Koketsu, Ritsuko" sort="Kubota Koketsu, Ritsuko" uniqKey="Kubota Koketsu R" first="Ritsuko" last="Kubota-Koketsu">Ritsuko Kubota-Koketsu</name><affiliation><nlm:aff id="aff3">Department of Virology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka, Japan</nlm:aff></affiliation></author><author><name sortKey="Ikeda, Mariko" sort="Ikeda, Mariko" uniqKey="Ikeda M" first="Mariko" last="Ikeda">Mariko Ikeda</name><affiliation><nlm:aff id="aff2">RIKEN Systems and Structural Biology Center, Suehiro, Tsurumi, Yokohama, Japan</nlm:aff></affiliation></author><author><name sortKey="Wakiyama, Motoaki" sort="Wakiyama, Motoaki" uniqKey="Wakiyama M" first="Motoaki" last="Wakiyama">Motoaki Wakiyama</name><affiliation><nlm:aff id="aff2">RIKEN Systems and Structural Biology Center, Suehiro, Tsurumi, Yokohama, Japan</nlm:aff></affiliation></author><author><name sortKey="Shirouzu, Mikako" sort="Shirouzu, Mikako" uniqKey="Shirouzu M" first="Mikako" last="Shirouzu">Mikako Shirouzu</name><affiliation><nlm:aff id="aff2">RIKEN Systems and Structural Biology Center, Suehiro, Tsurumi, Yokohama, Japan</nlm:aff></affiliation></author><author><name sortKey="Okada, Jun" sort="Okada, Jun" uniqKey="Okada J" first="Jun" last="Okada">Jun Okada</name><affiliation><nlm:aff id="aff4">Sales and Marketing Division, Medical and Biological Laboratories Co., Ltd., Nagoya, Aichi, Japan</nlm:aff></affiliation></author><author><name sortKey="Okuno, Yoshinobu" sort="Okuno, Yoshinobu" uniqKey="Okuno Y" first="Yoshinobu" last="Okuno">Yoshinobu Okuno</name><affiliation><nlm:aff id="aff5">Kanonji Institute, The Research Foundation for Microbial Diseases, Osaka University, Kanonji, Kagawa, Japan</nlm:aff></affiliation></author><author><name sortKey="Kurosawa, Yoshikazu" sort="Kurosawa, Yoshikazu" uniqKey="Kurosawa Y" first="Yoshikazu" last="Kurosawa">Yoshikazu Kurosawa</name><affiliation><nlm:aff id="aff1">Institute for Comprehensive Medical Science, Fujita Health University, Toyoake, Aichi, Japan</nlm:aff></affiliation></author><author><name sortKey="Yokoyama, Shigeyuki" sort="Yokoyama, Shigeyuki" uniqKey="Yokoyama S" first="Shigeyuki" last="Yokoyama">Shigeyuki Yokoyama</name><affiliation><nlm:aff id="aff2">RIKEN Systems and Structural Biology Center, Suehiro, Tsurumi, Yokohama, Japan</nlm:aff></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="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>ABSTRACT</title><p>Neutralizing antibodies that target the hemagglutinin of influenza virus either inhibit binding of hemagglutinin to cellular receptors or prevent the low-pH-induced conformational change in hemagglutinin required for membrane fusion. In general, the former type of antibody binds to the globular head formed by HA1 and has narrow strain specificity, while the latter type binds to the stem mainly formed by HA2 and has broad strain specificity. In the present study, we analyzed the epitope and function of a broadly neutralizing human antibody against H3N2 viruses, F005-126. The crystal structure of F005-126 Fab in complex with hemagglutinin revealed that the antibody binds to the globular head, spans a cleft formed by two hemagglutinin monomers in a hemagglutinin trimer, and cross-links them. It recognizes two peptide portions (sites L and R) and a glycan linked to asparagine at residue 285 using three complementarity-determining regions and framework 3 in the heavy chain. Binding of the antibody to sites L (residues 171 to 173, 239, and 240) and R (residues 91, 92, 270 to 273, 284, and 285) is mediated mainly by van der Waals contacts with the main chains of the peptides in these sites and secondarily by hydrogen bonds with a few side chains of conserved sequences in HA1. Furthermore, the glycan recognized by F005-126 is conserved among H3N2 viruses. F005-126 has the ability to prevent low-pH-induced conformational changes in hemagglutinin. The newly identified conserved epitope, including the glycan, should be immunogenic in humans and may induce production of broadly neutralizing antibodies against H3 viruses.</p><p><bold>IMPORTANCE</bold> Antibodies play an important role in protection against influenza virus, and hemagglutinin is the major target for virus neutralizing antibodies. It has long been believed that all effective neutralizing antibodies bind to the surrounding regions of the sialic acid-binding pocket and inhibit the binding of hemagglutinin to the cellular receptor. Since mutations are readily introduced into such epitopes, this type of antibody shows narrow strain specificity. Recently, however, broadly neutralizing antibodies have been isolated. Most of these bind either to conserved sites in the stem region or to the sialic acid-binding pocket itself. In the present study, we identified a new neutralizing epitope in the head region recognized by a broadly neutralizing human antibody against H3N2. This epitope may be useful for design of vaccines.</p></div></front></TEI><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>
<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">24719430</article-id><article-id pub-id-type="pmc">4054433</article-id><article-id pub-id-type="publisher-id">00420-14</article-id><article-id pub-id-type="doi">10.1128/JVI.00420-14</article-id><article-categories><subj-group subj-group-type="heading"><subject>Vaccines and Antiviral Agents</subject></subj-group></article-categories><title-group><article-title>Conserved Neutralizing Epitope at Globular Head of Hemagglutinin in H3N2 Influenza Viruses</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Iba</surname><given-names>Yoshitaka</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref></contrib><contrib contrib-type="author"><name><surname>Fujii</surname><given-names>Yoshifumi</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref><xref ref-type="author-notes" rid="fn1">*</xref></contrib><contrib contrib-type="author"><name><surname>Ohshima</surname><given-names>Nobuko</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref></contrib><contrib contrib-type="author"><name><surname>Sumida</surname><given-names>Tomomi</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref><xref ref-type="author-notes" rid="fn1">*</xref></contrib><contrib contrib-type="author"><name><surname>Kubota-Koketsu</surname><given-names>Ritsuko</given-names></name><xref ref-type="aff" rid="aff3"><sup>c</sup></xref></contrib><contrib contrib-type="author"><name><surname>Ikeda</surname><given-names>Mariko</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref><xref ref-type="author-notes" rid="fn1">*</xref></contrib><contrib contrib-type="author"><name><surname>Wakiyama</surname><given-names>Motoaki</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref><xref ref-type="author-notes" rid="fn1">*</xref></contrib><contrib contrib-type="author"><name><surname>Shirouzu</surname><given-names>Mikako</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref><xref ref-type="author-notes" rid="fn1">*</xref></contrib><contrib contrib-type="author"><name><surname>Okada</surname><given-names>Jun</given-names></name><xref ref-type="aff" rid="aff4"><sup>d</sup></xref></contrib><contrib contrib-type="author"><name><surname>Okuno</surname><given-names>Yoshinobu</given-names></name><xref ref-type="aff" rid="aff5"><sup>e</sup></xref></contrib><contrib contrib-type="author" corresp="yes"><name><surname>Kurosawa</surname><given-names>Yoshikazu</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref></contrib><contrib contrib-type="author"><name><surname>Yokoyama</surname><given-names>Shigeyuki</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref><xref ref-type="author-notes" rid="fn1">*</xref></contrib><aff id="aff1"><label>a</label>Institute for Comprehensive Medical Science, Fujita Health University, Toyoake, Aichi, Japan</aff><aff id="aff2"><label>b</label>RIKEN Systems and Structural Biology Center, Suehiro, Tsurumi, Yokohama, Japan</aff><aff id="aff3"><label>c</label>Department of Virology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka, Japan</aff><aff id="aff4"><label>d</label>Sales and Marketing Division, Medical and Biological Laboratories Co., Ltd., Nagoya, Aichi, Japan</aff><aff id="aff5"><label>e</label>Kanonji Institute, The Research Foundation for Microbial Diseases, Osaka University, Kanonji, Kagawa, Japan</aff></contrib-group><contrib-group><contrib contrib-type="editor"><name><surname>Dermody</surname><given-names>T. S.</given-names></name><role>Editor</role></contrib></contrib-group><author-notes><corresp id="cor1">Address correspondence to Yoshikazu Kurosawa, <email>kurosawa@fujita-hu.ac.jp</email>.</corresp><fn fn-type="equal"><p>Y.I. and Y.F. contributed equally to this article.</p></fn><fn id="fn1" fn-type="present-address"><label>*</label><p>Present address: Yoshifumi Fujii, RIKEN Structural Biology Laboratory, Suehiro, Tsurumi, Yokohama, Japan; Tomomi Sumida, RIKEN Structural Biology Laboratory, Suehiro, Tsurumi, Yokohama, Japan; Mariko Ikeda, RIKEN Center for Life Science Technologies, Suehiro, Tsurumi, Yokohama, Japan; Motoaki Wakiyama, RIKEN Center for Life Science Technologies, Suehiro, Tsurumi, Yokohama, Japan; Mikako Shirouzu, RIKEN Center for Life Science Technologies, Suehiro, Tsurumi, Yokohama, Japan; Shigeyuki Yokoyama, RIKEN Structural Biology Laboratory, Suehiro, Tsurumi, Yokohama, Japan.</p></fn></author-notes><pub-date pub-type="ppub"><month>7</month><year>2014</year></pub-date><pub-date pub-type="pmc-release"><day>1</day><month>7</month><year>2014</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on the
<volume>88</volume><issue>13</issue><fpage>7130</fpage><lpage>7144</lpage><history><date date-type="received"><day>11</day><month>2</month><year>2014</year></date><date date-type="accepted"><day>3</day><month>4</month><year>2014</year></date></history><permissions><copyright-statement>Copyright © 2014, American Society for Microbiology. All Rights Reserved.</copyright-statement><copyright-year>2014</copyright-year><copyright-holder>American Society for Microbiology</copyright-holder><license license-type="open-access"><license-p>The authors have paid a fee to allow immediate free access to this article.</license-p></license></permissions><self-uri xlink:title="pdf" xlink:type="simple" xlink:href="zjv01314007130.pdf"></self-uri><abstract><title>ABSTRACT</title><p>Neutralizing antibodies that target the hemagglutinin of influenza virus either inhibit binding of hemagglutinin to cellular receptors or prevent the low-pH-induced conformational change in hemagglutinin required for membrane fusion. In general, the former type of antibody binds to the globular head formed by HA1 and has narrow strain specificity, while the latter type binds to the stem mainly formed by HA2 and has broad strain specificity. In the present study, we analyzed the epitope and function of a broadly neutralizing human antibody against H3N2 viruses, F005-126. The crystal structure of F005-126 Fab in complex with hemagglutinin revealed that the antibody binds to the globular head, spans a cleft formed by two hemagglutinin monomers in a hemagglutinin trimer, and cross-links them. It recognizes two peptide portions (sites L and R) and a glycan linked to asparagine at residue 285 using three complementarity-determining regions and framework 3 in the heavy chain. Binding of the antibody to sites L (residues 171 to 173, 239, and 240) and R (residues 91, 92, 270 to 273, 284, and 285) is mediated mainly by van der Waals contacts with the main chains of the peptides in these sites and secondarily by hydrogen bonds with a few side chains of conserved sequences in HA1. Furthermore, the glycan recognized by F005-126 is conserved among H3N2 viruses. F005-126 has the ability to prevent low-pH-induced conformational changes in hemagglutinin. The newly identified conserved epitope, including the glycan, should be immunogenic in humans and may induce production of broadly neutralizing antibodies against H3 viruses.</p><p><bold>IMPORTANCE</bold> Antibodies play an important role in protection against influenza virus, and hemagglutinin is the major target for virus neutralizing antibodies. It has long been believed that all effective neutralizing antibodies bind to the surrounding regions of the sialic acid-binding pocket and inhibit the binding of hemagglutinin to the cellular receptor. Since mutations are readily introduced into such epitopes, this type of antibody shows narrow strain specificity. Recently, however, broadly neutralizing antibodies have been isolated. Most of these bind either to conserved sites in the stem region or to the sialic acid-binding pocket itself. In the present study, we identified a new neutralizing epitope in the head region recognized by a broadly neutralizing human antibody against H3N2. This epitope may be useful for design of vaccines.</p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/H2N2V1/Data/Pmc/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000683 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Pmc/Corpus/biblio.hfd -nk 000683 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= H2N2V1
|flux= Pmc
|étape= Corpus
|type= RBID
|clé=
|texte=
}}
| This area was generated with Dilib version V0.6.33. |  |