A Human Antibody Recognizing a Conserved Epitope of H5 Hemagglutinin Broadly Neutralizes Highly Pathogenic Avian Influenza H5N1 Viruses
Identifieur interne : 000644 ( Pmc/Corpus ); précédent : 000643; suivant : 000645A Human Antibody Recognizing a Conserved Epitope of H5 Hemagglutinin Broadly Neutralizes Highly Pathogenic Avian Influenza H5N1 Viruses
Auteurs : Hongxing Hu ; Jarrod Voss ; Guoliang Zhang ; Philippi Buchy ; Teng Zuo ; Lulan Wang ; Feng Wang ; Fan Zhou ; Guiqing Wang ; Cheguo Tsai ; Lesley Calder ; Steve J. Gamblin ; Linqi Zhang ; Vincent Deubel ; Boping Zhou ; John J. Skehel ; Paul ZhouSource :
- Journal of Virology [ 0022-538X ] ; 2012.
Abstract
Influenza A virus infection is a persistent threat to public health worldwide due to its ability to evade immune surveillance through rapid genetic drift and shift. Current vaccines against influenza A virus provide immunity to viral isolates that are similar to vaccine strains. High-affinity neutralizing antibodies against conserved epitopes could provide immunity to diverse influenza virus strains and protection against future pandemic viruses. In this study, by using a highly sensitive H5N1 pseudotype-based neutralization assay to screen human monoclonal antibodies produced by memory B cells from an H5N1-infected individual and molecular cloning techniques, we developed three fully human monoclonal antibodies. Among them, antibody 65C6 exhibited potent neutralization activity against all H5 clades and subclades except for subclade 7.2 and prophylactic and therapeutic efficacy against highly pathogenic avian influenza H5N1 viruses in mice. Studies on hemagglutinin (HA)-antibody complexes by electron microscopy and epitope mapping indicate that antibody 65C6 binds to a conformational epitope comprising amino acid residues at positions 118, 121, 161, 164, and 167 (according to mature H5 numbering) on the tip of the membrane-distal globular domain of HA. Thus, we conclude that antibody 65C6 recognizes a neutralization epitope in the globular head of HA that is conserved among almost all divergent H5N1 influenza stains.
Url:
DOI: 10.1128/JVI.06665-11
PubMed: 22238297
PubMed Central: 3302345
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PMC:3302345Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">A Human Antibody Recognizing a Conserved Epitope of H5 Hemagglutinin Broadly Neutralizes Highly Pathogenic Avian Influenza H5N1 Viruses</title>
<author><name sortKey="Hu, Hongxing" sort="Hu, Hongxing" uniqKey="Hu H" first="Hongxing" last="Hu">Hongxing Hu</name>
<affiliation><nlm:aff id="aff1">Unit of Anti-Viral Immunity and Genetic Therapy, Key Laboratory of Molecular Virology and Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, Shanghai, China</nlm:aff>
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<author><name sortKey="Voss, Jarrod" sort="Voss, Jarrod" uniqKey="Voss J" first="Jarrod" last="Voss">Jarrod Voss</name>
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<author><name sortKey="Zhang, Guoliang" sort="Zhang, Guoliang" uniqKey="Zhang G" first="Guoliang" last="Zhang">Guoliang Zhang</name>
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<author><name sortKey="Buchy, Philippi" sort="Buchy, Philippi" uniqKey="Buchy P" first="Philippi" last="Buchy">Philippi Buchy</name>
<affiliation><nlm:aff id="aff4">Institut Pasteur in Cambodia, Phnom Penh, Cambodia</nlm:aff>
</affiliation>
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<author><name sortKey="Zuo, Teng" sort="Zuo, Teng" uniqKey="Zuo T" first="Teng" last="Zuo">Teng Zuo</name>
<affiliation><nlm:aff id="aff5">Comprehensive AIDS Research Center, School of Medicine, Tsinghua University, Beijing, China</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Wang, Lulan" sort="Wang, Lulan" uniqKey="Wang L" first="Lulan" last="Wang">Lulan Wang</name>
<affiliation><nlm:aff id="aff1">Unit of Anti-Viral Immunity and Genetic Therapy, Key Laboratory of Molecular Virology and Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, Shanghai, China</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Wang, Feng" sort="Wang, Feng" uniqKey="Wang F" first="Feng" last="Wang">Feng Wang</name>
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</affiliation>
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<author><name sortKey="Zhou, Fan" sort="Zhou, Fan" uniqKey="Zhou F" first="Fan" last="Zhou">Fan Zhou</name>
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</affiliation>
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<author><name sortKey="Wang, Guiqing" sort="Wang, Guiqing" uniqKey="Wang G" first="Guiqing" last="Wang">Guiqing Wang</name>
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<author><name sortKey="Tsai, Cheguo" sort="Tsai, Cheguo" uniqKey="Tsai C" first="Cheguo" last="Tsai">Cheguo Tsai</name>
<affiliation><nlm:aff id="aff1">Unit of Anti-Viral Immunity and Genetic Therapy, Key Laboratory of Molecular Virology and Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, Shanghai, China</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Calder, Lesley" sort="Calder, Lesley" uniqKey="Calder L" first="Lesley" last="Calder">Lesley Calder</name>
<affiliation><nlm:aff id="aff2">National Institute for Medical Research, London, United Kingdom</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Gamblin, Steve J" sort="Gamblin, Steve J" uniqKey="Gamblin S" first="Steve J." last="Gamblin">Steve J. Gamblin</name>
<affiliation><nlm:aff id="aff2">National Institute for Medical Research, London, United Kingdom</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Zhang, Linqi" sort="Zhang, Linqi" uniqKey="Zhang L" first="Linqi" last="Zhang">Linqi Zhang</name>
<affiliation><nlm:aff id="aff5">Comprehensive AIDS Research Center, School of Medicine, Tsinghua University, Beijing, China</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Deubel, Vincent" sort="Deubel, Vincent" uniqKey="Deubel V" first="Vincent" last="Deubel">Vincent Deubel</name>
<affiliation><nlm:aff id="aff4">Institut Pasteur in Cambodia, Phnom Penh, Cambodia</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Zhou, Boping" sort="Zhou, Boping" uniqKey="Zhou B" first="Boping" last="Zhou">Boping Zhou</name>
<affiliation><nlm:aff id="aff3">Shenzhen Third Hospital, Shenzhen, China</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Skehel, John J" sort="Skehel, John J" uniqKey="Skehel J" first="John J." last="Skehel">John J. Skehel</name>
<affiliation><nlm:aff id="aff2">National Institute for Medical Research, London, United Kingdom</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Zhou, Paul" sort="Zhou, Paul" uniqKey="Zhou P" first="Paul" last="Zhou">Paul Zhou</name>
<affiliation><nlm:aff id="aff1">Unit of Anti-Viral Immunity and Genetic Therapy, Key Laboratory of Molecular Virology and Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, Shanghai, China</nlm:aff>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">A Human Antibody Recognizing a Conserved Epitope of H5 Hemagglutinin Broadly Neutralizes Highly Pathogenic Avian Influenza H5N1 Viruses</title>
<author><name sortKey="Hu, Hongxing" sort="Hu, Hongxing" uniqKey="Hu H" first="Hongxing" last="Hu">Hongxing Hu</name>
<affiliation><nlm:aff id="aff1">Unit of Anti-Viral Immunity and Genetic Therapy, Key Laboratory of Molecular Virology and Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, Shanghai, China</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Voss, Jarrod" sort="Voss, Jarrod" uniqKey="Voss J" first="Jarrod" last="Voss">Jarrod Voss</name>
<affiliation><nlm:aff id="aff2">National Institute for Medical Research, London, United Kingdom</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Zhang, Guoliang" sort="Zhang, Guoliang" uniqKey="Zhang G" first="Guoliang" last="Zhang">Guoliang Zhang</name>
<affiliation><nlm:aff id="aff3">Shenzhen Third Hospital, Shenzhen, China</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Buchy, Philippi" sort="Buchy, Philippi" uniqKey="Buchy P" first="Philippi" last="Buchy">Philippi Buchy</name>
<affiliation><nlm:aff id="aff4">Institut Pasteur in Cambodia, Phnom Penh, Cambodia</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Zuo, Teng" sort="Zuo, Teng" uniqKey="Zuo T" first="Teng" last="Zuo">Teng Zuo</name>
<affiliation><nlm:aff id="aff5">Comprehensive AIDS Research Center, School of Medicine, Tsinghua University, Beijing, China</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Wang, Lulan" sort="Wang, Lulan" uniqKey="Wang L" first="Lulan" last="Wang">Lulan Wang</name>
<affiliation><nlm:aff id="aff1">Unit of Anti-Viral Immunity and Genetic Therapy, Key Laboratory of Molecular Virology and Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, Shanghai, China</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Wang, Feng" sort="Wang, Feng" uniqKey="Wang F" first="Feng" last="Wang">Feng Wang</name>
<affiliation><nlm:aff id="aff1">Unit of Anti-Viral Immunity and Genetic Therapy, Key Laboratory of Molecular Virology and Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, Shanghai, China</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Zhou, Fan" sort="Zhou, Fan" uniqKey="Zhou F" first="Fan" last="Zhou">Fan Zhou</name>
<affiliation><nlm:aff id="aff1">Unit of Anti-Viral Immunity and Genetic Therapy, Key Laboratory of Molecular Virology and Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, Shanghai, China</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Wang, Guiqing" sort="Wang, Guiqing" uniqKey="Wang G" first="Guiqing" last="Wang">Guiqing Wang</name>
<affiliation><nlm:aff id="aff1">Unit of Anti-Viral Immunity and Genetic Therapy, Key Laboratory of Molecular Virology and Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, Shanghai, China</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Tsai, Cheguo" sort="Tsai, Cheguo" uniqKey="Tsai C" first="Cheguo" last="Tsai">Cheguo Tsai</name>
<affiliation><nlm:aff id="aff1">Unit of Anti-Viral Immunity and Genetic Therapy, Key Laboratory of Molecular Virology and Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, Shanghai, China</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Calder, Lesley" sort="Calder, Lesley" uniqKey="Calder L" first="Lesley" last="Calder">Lesley Calder</name>
<affiliation><nlm:aff id="aff2">National Institute for Medical Research, London, United Kingdom</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Gamblin, Steve J" sort="Gamblin, Steve J" uniqKey="Gamblin S" first="Steve J." last="Gamblin">Steve J. Gamblin</name>
<affiliation><nlm:aff id="aff2">National Institute for Medical Research, London, United Kingdom</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Zhang, Linqi" sort="Zhang, Linqi" uniqKey="Zhang L" first="Linqi" last="Zhang">Linqi Zhang</name>
<affiliation><nlm:aff id="aff5">Comprehensive AIDS Research Center, School of Medicine, Tsinghua University, Beijing, China</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Deubel, Vincent" sort="Deubel, Vincent" uniqKey="Deubel V" first="Vincent" last="Deubel">Vincent Deubel</name>
<affiliation><nlm:aff id="aff4">Institut Pasteur in Cambodia, Phnom Penh, Cambodia</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Zhou, Boping" sort="Zhou, Boping" uniqKey="Zhou B" first="Boping" last="Zhou">Boping Zhou</name>
<affiliation><nlm:aff id="aff3">Shenzhen Third Hospital, Shenzhen, China</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Skehel, John J" sort="Skehel, John J" uniqKey="Skehel J" first="John J." last="Skehel">John J. Skehel</name>
<affiliation><nlm:aff id="aff2">National Institute for Medical Research, London, United Kingdom</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Zhou, Paul" sort="Zhou, Paul" uniqKey="Zhou P" first="Paul" last="Zhou">Paul Zhou</name>
<affiliation><nlm:aff id="aff1">Unit of Anti-Viral Immunity and Genetic Therapy, Key Laboratory of Molecular Virology and Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, Shanghai, China</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="2012">2012</date>
</imprint>
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<front><div type="abstract" xml:lang="en"><p>Influenza A virus infection is a persistent threat to public health worldwide due to its ability to evade immune surveillance through rapid genetic drift and shift. Current vaccines against influenza A virus provide immunity to viral isolates that are similar to vaccine strains. High-affinity neutralizing antibodies against conserved epitopes could provide immunity to diverse influenza virus strains and protection against future pandemic viruses. In this study, by using a highly sensitive H5N1 pseudotype-based neutralization assay to screen human monoclonal antibodies produced by memory B cells from an H5N1-infected individual and molecular cloning techniques, we developed three fully human monoclonal antibodies. Among them, antibody 65C6 exhibited potent neutralization activity against all H5 clades and subclades except for subclade 7.2 and prophylactic and therapeutic efficacy against highly pathogenic avian influenza H5N1 viruses in mice. Studies on hemagglutinin (HA)-antibody complexes by electron microscopy and epitope mapping indicate that antibody 65C6 binds to a conformational epitope comprising amino acid residues at positions 118, 121, 161, 164, and 167 (according to mature H5 numbering) on the tip of the membrane-distal globular domain of HA. Thus, we conclude that antibody 65C6 recognizes a neutralization epitope in the globular head of HA that is conserved among almost all divergent H5N1 influenza stains.</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="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">22238297</article-id>
<article-id pub-id-type="pmc">3302345</article-id>
<article-id pub-id-type="publisher-id">06665-11</article-id>
<article-id pub-id-type="doi">10.1128/JVI.06665-11</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Pathogenesis and Immunity</subject>
</subj-group>
</article-categories>
<title-group><article-title>A Human Antibody Recognizing a Conserved Epitope of H5 Hemagglutinin Broadly Neutralizes Highly Pathogenic Avian Influenza H5N1 Viruses</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Hu</surname>
<given-names>Hongxing</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>a</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Voss</surname>
<given-names>Jarrod</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>b</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Zhang</surname>
<given-names>Guoliang</given-names>
</name>
<xref ref-type="aff" rid="aff3"><sup>c</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Buchy</surname>
<given-names>Philippi</given-names>
</name>
<xref ref-type="aff" rid="aff4"><sup>d</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Zuo</surname>
<given-names>Teng</given-names>
</name>
<xref ref-type="aff" rid="aff5"><sup>e</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Wang</surname>
<given-names>Lulan</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>a</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Wang</surname>
<given-names>Feng</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>a</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Zhou</surname>
<given-names>Fan</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>a</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Wang</surname>
<given-names>Guiqing</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>a</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Tsai</surname>
<given-names>Cheguo</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>a</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Calder</surname>
<given-names>Lesley</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>b</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Gamblin</surname>
<given-names>Steve J.</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>b</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Zhang</surname>
<given-names>Linqi</given-names>
</name>
<xref ref-type="aff" rid="aff5"><sup>e</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Deubel</surname>
<given-names>Vincent</given-names>
</name>
<xref ref-type="aff" rid="aff4"><sup>d</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Zhou</surname>
<given-names>Boping</given-names>
</name>
<xref ref-type="aff" rid="aff3"><sup>c</sup>
</xref>
</contrib>
<contrib contrib-type="author" corresp="yes"><name><surname>Skehel</surname>
<given-names>John J.</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>b</sup>
</xref>
</contrib>
<contrib contrib-type="author" corresp="yes"><name><surname>Zhou</surname>
<given-names>Paul</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>a</sup>
</xref>
</contrib>
<aff id="aff1"><label>a</label>
Unit of Anti-Viral Immunity and Genetic Therapy, Key Laboratory of Molecular Virology and Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, Shanghai, China</aff>
<aff id="aff2"><label>b</label>
National Institute for Medical Research, London, United Kingdom</aff>
<aff id="aff3"><label>c</label>
Shenzhen Third Hospital, Shenzhen, China</aff>
<aff id="aff4"><label>d</label>
Institut Pasteur in Cambodia, Phnom Penh, Cambodia</aff>
<aff id="aff5"><label>e</label>
Comprehensive AIDS Research Center, School of Medicine, Tsinghua University, Beijing, China</aff>
</contrib-group>
<author-notes><corresp>Address correspondence to Paul Zhou, <email>blzhou@sibs.ac.cn</email>
, or John J. Skehel, <email>skeheljj@nimr.mrc.ac.uk</email>
.</corresp>
</author-notes>
<pub-date pub-type="ppub"><month>3</month>
<year>2012</year>
</pub-date>
<volume>86</volume>
<issue>6</issue>
<fpage>2978</fpage>
<lpage>2989</lpage>
<history><date date-type="received"><day>26</day>
<month>10</month>
<year>2011</year>
</date>
<date date-type="accepted"><day>22</day>
<month>12</month>
<year>2011</year>
</date>
</history>
<permissions><copyright-statement>Copyright © 2012, American Society for Microbiology. All Rights Reserved.</copyright-statement>
<copyright-year>2012</copyright-year>
<copyright-holder>American Society for Microbiology</copyright-holder>
</permissions>
<self-uri xlink:title="pdf" xlink:type="simple" xlink:href="zjv00612002978.pdf"></self-uri>
<abstract><p>Influenza A virus infection is a persistent threat to public health worldwide due to its ability to evade immune surveillance through rapid genetic drift and shift. Current vaccines against influenza A virus provide immunity to viral isolates that are similar to vaccine strains. High-affinity neutralizing antibodies against conserved epitopes could provide immunity to diverse influenza virus strains and protection against future pandemic viruses. In this study, by using a highly sensitive H5N1 pseudotype-based neutralization assay to screen human monoclonal antibodies produced by memory B cells from an H5N1-infected individual and molecular cloning techniques, we developed three fully human monoclonal antibodies. Among them, antibody 65C6 exhibited potent neutralization activity against all H5 clades and subclades except for subclade 7.2 and prophylactic and therapeutic efficacy against highly pathogenic avian influenza H5N1 viruses in mice. Studies on hemagglutinin (HA)-antibody complexes by electron microscopy and epitope mapping indicate that antibody 65C6 binds to a conformational epitope comprising amino acid residues at positions 118, 121, 161, 164, and 167 (according to mature H5 numbering) on the tip of the membrane-distal globular domain of HA. Thus, we conclude that antibody 65C6 recognizes a neutralization epitope in the globular head of HA that is conserved among almost all divergent H5N1 influenza stains.</p>
</abstract>
</article-meta>
</front>
</pmc>
</record>
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