Antibody recognition of a highly conserved influenza virus epitope: implications for universal prevention and therapy
Identifieur interne : 000838 ( Ncbi/Merge ); précédent : 000837; suivant : 000839Antibody recognition of a highly conserved influenza virus epitope: implications for universal prevention and therapy
Auteurs : Damian C. Ekiert [États-Unis] ; Gira Bhabha [États-Unis] ; Marc-André Elsliger [États-Unis] ; Robert H. E. Friesen [Pays-Bas] ; Mandy Jongeneelen [Pays-Bas] ; Mark Throsby [Pays-Bas] ; Jaap Goudsmit [Pays-Bas] ; Ian A. Wilson [États-Unis]Source :
- Science (New York, N.Y.) [ 0036-8075 ] ; 2009.
Descripteurs français
- KwdFr :
- Affinité des anticorps, Anticorps antiviraux (), Anticorps antiviraux (immunologie), Antigènes viraux (), Antigènes viraux (immunologie), Concentration en ions d'hydrogène, Conformation des protéines, Cristallisation, Cristallographie aux rayons X, Fragments Fab d'immunoglobuline (), Fragments Fab d'immunoglobuline (immunologie), Fusion membranaire, Glycoprotéine hémagglutinine du virus influenza (), Glycoprotéine hémagglutinine du virus influenza (immunologie), Glycosylation, Humains, Interactions hydrophobes et hydrophiles, Liaison hydrogène, Modèles moléculaires, Sites de fixation des anticorps, Sous-type H1N1 du virus de la grippe A (immunologie), Sous-type H5N1 du virus de la grippe A (immunologie), Structure secondaire des protéines, Structure tertiaire des protéines, Tests de neutralisation, Vaccins antigrippaux, Épitopes (immunologie).
- MESH :
- immunologie : Anticorps antiviraux, Antigènes viraux, Fragments Fab d'immunoglobuline, Glycoprotéine hémagglutinine du virus influenza, Sous-type H1N1 du virus de la grippe A, Sous-type H5N1 du virus de la grippe A, Épitopes.
- Affinité des anticorps, Anticorps antiviraux, Antigènes viraux, Concentration en ions d'hydrogène, Conformation des protéines, Cristallisation, Cristallographie aux rayons X, Fragments Fab d'immunoglobuline, Fusion membranaire, Glycoprotéine hémagglutinine du virus influenza, Glycosylation, Humains, Interactions hydrophobes et hydrophiles, Liaison hydrogène, Modèles moléculaires, Sites de fixation des anticorps, Structure secondaire des protéines, Structure tertiaire des protéines, Tests de neutralisation, Vaccins antigrippaux.
English descriptors
- KwdEn :
- Antibodies, Viral (chemistry), Antibodies, Viral (immunology), Antibody Affinity, Antigens, Viral (chemistry), Antigens, Viral (immunology), Binding Sites, Antibody, Crystallization, Crystallography, X-Ray, Epitopes (immunology), Glycosylation, Hemagglutinin Glycoproteins, Influenza Virus (chemistry), Hemagglutinin Glycoproteins, Influenza Virus (immunology), Humans, Hydrogen Bonding, Hydrogen-Ion Concentration, Hydrophobic and Hydrophilic Interactions, Immunoglobulin Fab Fragments (chemistry), Immunoglobulin Fab Fragments (immunology), Influenza A Virus, H1N1 Subtype (immunology), Influenza A Virus, H5N1 Subtype (immunology), Influenza Vaccines, Membrane Fusion, Models, Molecular, Neutralization Tests, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary.
- MESH :
- chemical , chemistry : Antibodies, Viral, Antigens, Viral, Hemagglutinin Glycoproteins, Influenza Virus, Immunoglobulin Fab Fragments.
- chemical , immunology : Antibodies, Viral, Antigens, Viral, Epitopes, Hemagglutinin Glycoproteins, Influenza Virus, Immunoglobulin Fab Fragments.
- immunology : Influenza A Virus, H1N1 Subtype, Influenza A Virus, H5N1 Subtype.
- Antibody Affinity, Binding Sites, Antibody, Crystallization, Crystallography, X-Ray, Glycosylation, Humans, Hydrogen Bonding, Hydrogen-Ion Concentration, Hydrophobic and Hydrophilic Interactions, Influenza Vaccines, Membrane Fusion, Models, Molecular, Neutralization Tests, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary.
Abstract
Influenza virus presents a significant and persistent threat to public health worldwide and current vaccines provide immunity to viral isolates similar to the vaccine strain. High affinity antibodies against a conserved epitope could provide immunity to the diverse influenza subtypes and protection against future pandemic viruses. Co-crystal structures were determined at 2.2 and 2.7 Å resolutions for broadly neutralizing human antibody CR6261 Fab in complexes with the major surface antigen (hemagglutinin, HA) from viruses responsible for the 1918 H1N1 influenza pandemic and a recent lethal case of H5N1 avian influenza. In contrast to all other structurally characterized influenza antibodies, CR6261 recognizes a highly conserved helical region in the membrane-proximal stem of HA1/HA2. The antibody neutralizes the virus by blocking conformational rearrangements associated with membrane fusion. The CR6261 epitope identified here should accelerate the design and implementation of improved vaccines that can elicit CR6261-like antibodies, as well as antibody-based therapies for the treatment of influenza.
Url:
DOI: 10.1126/science.1171491
PubMed: 19251591
PubMed Central: 2758658
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PMC:2758658Le document en format XML
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E." last="Friesen">Robert H. E. Friesen</name><affiliation wicri:level="1"><nlm:aff id="A2">Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden, The Netherlands</nlm:aff><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden</wicri:regionArea><wicri:noRegion>2301 CA Leiden</wicri:noRegion></affiliation></author><author><name sortKey="Jongeneelen, Mandy" sort="Jongeneelen, Mandy" uniqKey="Jongeneelen M" first="Mandy" last="Jongeneelen">Mandy Jongeneelen</name><affiliation wicri:level="1"><nlm:aff id="A2">Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden, The Netherlands</nlm:aff><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden</wicri:regionArea><wicri:noRegion>2301 CA Leiden</wicri:noRegion></affiliation></author><author><name sortKey="Throsby, Mark" sort="Throsby, Mark" uniqKey="Throsby M" first="Mark" last="Throsby">Mark Throsby</name><affiliation wicri:level="1"><nlm:aff id="A2">Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden, The Netherlands</nlm:aff><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden</wicri:regionArea><wicri:noRegion>2301 CA Leiden</wicri:noRegion></affiliation></author><author><name sortKey="Goudsmit, Jaap" sort="Goudsmit, Jaap" uniqKey="Goudsmit J" first="Jaap" last="Goudsmit">Jaap Goudsmit</name><affiliation wicri:level="1"><nlm:aff id="A2">Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden, The Netherlands</nlm:aff><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden</wicri:regionArea><wicri:noRegion>2301 CA Leiden</wicri:noRegion></affiliation></author><author><name sortKey="Wilson, Ian A" sort="Wilson, Ian A" uniqKey="Wilson I" first="Ian A." last="Wilson">Ian A. Wilson</name><affiliation wicri:level="2"><nlm:aff id="A1">Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.</nlm:aff><country xml:lang="fr" wicri:curation="lc">États-Unis</country><wicri:regionArea>Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation><affiliation wicri:level="2"><nlm:aff id="A3">The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.</nlm:aff><country xml:lang="fr" wicri:curation="lc">États-Unis</country><wicri:regionArea>The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author></analytic><series><title level="j">Science (New York, N.Y.)</title><idno type="ISSN">0036-8075</idno><idno type="eISSN">1095-9203</idno><imprint><date when="2009">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antibodies, Viral (chemistry)</term><term>Antibodies, Viral (immunology)</term><term>Antibody Affinity</term><term>Antigens, Viral (chemistry)</term><term>Antigens, Viral (immunology)</term><term>Binding Sites, Antibody</term><term>Crystallization</term><term>Crystallography, X-Ray</term><term>Epitopes (immunology)</term><term>Glycosylation</term><term>Hemagglutinin Glycoproteins, Influenza Virus (chemistry)</term><term>Hemagglutinin Glycoproteins, Influenza Virus (immunology)</term><term>Humans</term><term>Hydrogen Bonding</term><term>Hydrogen-Ion Concentration</term><term>Hydrophobic and Hydrophilic Interactions</term><term>Immunoglobulin Fab Fragments (chemistry)</term><term>Immunoglobulin Fab Fragments (immunology)</term><term>Influenza A Virus, H1N1 Subtype (immunology)</term><term>Influenza A Virus, H5N1 Subtype (immunology)</term><term>Influenza Vaccines</term><term>Membrane Fusion</term><term>Models, Molecular</term><term>Neutralization Tests</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Affinité des anticorps</term><term>Anticorps antiviraux ()</term><term>Anticorps antiviraux (immunologie)</term><term>Antigènes viraux ()</term><term>Antigènes viraux (immunologie)</term><term>Concentration en ions d'hydrogène</term><term>Conformation des protéines</term><term>Cristallisation</term><term>Cristallographie aux rayons X</term><term>Fragments Fab d'immunoglobuline ()</term><term>Fragments Fab d'immunoglobuline (immunologie)</term><term>Fusion membranaire</term><term>Glycoprotéine hémagglutinine du virus influenza ()</term><term>Glycoprotéine hémagglutinine du virus influenza (immunologie)</term><term>Glycosylation</term><term>Humains</term><term>Interactions hydrophobes et hydrophiles</term><term>Liaison hydrogène</term><term>Modèles moléculaires</term><term>Sites de fixation des anticorps</term><term>Sous-type H1N1 du virus de la grippe A (immunologie)</term><term>Sous-type H5N1 du virus de la grippe A (immunologie)</term><term>Structure secondaire des protéines</term><term>Structure tertiaire des protéines</term><term>Tests de neutralisation</term><term>Vaccins antigrippaux</term><term>Épitopes (immunologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antibodies, Viral</term><term>Antigens, Viral</term><term>Hemagglutinin Glycoproteins, Influenza Virus</term><term>Immunoglobulin Fab Fragments</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Viral</term><term>Antigens, Viral</term><term>Epitopes</term><term>Hemagglutinin Glycoproteins, Influenza Virus</term><term>Immunoglobulin Fab Fragments</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Anticorps antiviraux</term><term>Antigènes viraux</term><term>Fragments Fab d'immunoglobuline</term><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Sous-type H1N1 du virus de la grippe A</term><term>Sous-type H5N1 du virus de la grippe A</term><term>Épitopes</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Influenza A Virus, H1N1 Subtype</term><term>Influenza A Virus, H5N1 Subtype</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Antibody Affinity</term><term>Binding Sites, Antibody</term><term>Crystallization</term><term>Crystallography, X-Ray</term><term>Glycosylation</term><term>Humans</term><term>Hydrogen Bonding</term><term>Hydrogen-Ion Concentration</term><term>Hydrophobic and Hydrophilic Interactions</term><term>Influenza Vaccines</term><term>Membrane Fusion</term><term>Models, Molecular</term><term>Neutralization Tests</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Affinité des anticorps</term><term>Anticorps antiviraux</term><term>Antigènes viraux</term><term>Concentration en ions d'hydrogène</term><term>Conformation des protéines</term><term>Cristallisation</term><term>Cristallographie aux rayons X</term><term>Fragments Fab d'immunoglobuline</term><term>Fusion membranaire</term><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Glycosylation</term><term>Humains</term><term>Interactions hydrophobes et hydrophiles</term><term>Liaison hydrogène</term><term>Modèles moléculaires</term><term>Sites de fixation des anticorps</term><term>Structure secondaire des protéines</term><term>Structure tertiaire des protéines</term><term>Tests de neutralisation</term><term>Vaccins antigrippaux</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="P1">Influenza virus presents a significant and persistent threat to public health worldwide and current vaccines provide immunity to viral isolates similar to the vaccine strain. High affinity antibodies against a conserved epitope could provide immunity to the diverse influenza subtypes and protection against future pandemic viruses. Co-crystal structures were determined at 2.2 and 2.7 Å resolutions for broadly neutralizing human antibody CR6261 Fab in complexes with the major surface antigen (hemagglutinin, HA) from viruses responsible for the 1918 H1N1 influenza pandemic and a recent lethal case of H5N1 avian influenza. In contrast to all other structurally characterized influenza antibodies, CR6261 recognizes a highly conserved helical region in the membrane-proximal stem of HA1/HA2. The antibody neutralizes the virus by blocking conformational rearrangements associated with membrane fusion. The CR6261 epitope identified here should accelerate the design and implementation of improved vaccines that can elicit CR6261-like antibodies, as well as antibody-based therapies for the treatment of influenza.</p></div></front></TEI><double pmid="19251591"><pmc><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Antibody recognition of a highly conserved influenza virus epitope: implications for universal prevention and therapy</title><author><name sortKey="Ekiert, Damian C" sort="Ekiert, Damian C" uniqKey="Ekiert D" first="Damian C." last="Ekiert">Damian C. Ekiert</name><affiliation wicri:level="2"><nlm:aff id="A1">Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.</nlm:aff><country xml:lang="fr" wicri:curation="lc">États-Unis</country><wicri:regionArea>Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author><author><name sortKey="Bhabha, Gira" sort="Bhabha, Gira" uniqKey="Bhabha G" first="Gira" last="Bhabha">Gira Bhabha</name><affiliation wicri:level="2"><nlm:aff id="A1">Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.</nlm:aff><country xml:lang="fr" wicri:curation="lc">États-Unis</country><wicri:regionArea>Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author><author><name sortKey="Elsliger, Marc Andre" sort="Elsliger, Marc Andre" uniqKey="Elsliger M" first="Marc-André" last="Elsliger">Marc-André Elsliger</name><affiliation wicri:level="2"><nlm:aff id="A1">Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.</nlm:aff><country xml:lang="fr" wicri:curation="lc">États-Unis</country><wicri:regionArea>Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author><author><name sortKey="Friesen, Robert H E" sort="Friesen, Robert H E" uniqKey="Friesen R" first="Robert H. E." last="Friesen">Robert H. E. Friesen</name><affiliation wicri:level="1"><nlm:aff id="A2">Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden, The Netherlands</nlm:aff><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden</wicri:regionArea><wicri:noRegion>2301 CA Leiden</wicri:noRegion></affiliation></author><author><name sortKey="Jongeneelen, Mandy" sort="Jongeneelen, Mandy" uniqKey="Jongeneelen M" first="Mandy" last="Jongeneelen">Mandy Jongeneelen</name><affiliation wicri:level="1"><nlm:aff id="A2">Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden, The Netherlands</nlm:aff><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden</wicri:regionArea><wicri:noRegion>2301 CA Leiden</wicri:noRegion></affiliation></author><author><name sortKey="Throsby, Mark" sort="Throsby, Mark" uniqKey="Throsby M" first="Mark" last="Throsby">Mark Throsby</name><affiliation wicri:level="1"><nlm:aff id="A2">Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden, The Netherlands</nlm:aff><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden</wicri:regionArea><wicri:noRegion>2301 CA Leiden</wicri:noRegion></affiliation></author><author><name sortKey="Goudsmit, Jaap" sort="Goudsmit, Jaap" uniqKey="Goudsmit J" first="Jaap" last="Goudsmit">Jaap Goudsmit</name><affiliation wicri:level="1"><nlm:aff id="A2">Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden, The Netherlands</nlm:aff><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden</wicri:regionArea><wicri:noRegion>2301 CA Leiden</wicri:noRegion></affiliation></author><author><name sortKey="Wilson, Ian A" sort="Wilson, Ian A" uniqKey="Wilson I" first="Ian A." last="Wilson">Ian A. Wilson</name><affiliation wicri:level="2"><nlm:aff id="A1">Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.</nlm:aff><country xml:lang="fr" wicri:curation="lc">États-Unis</country><wicri:regionArea>Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation><affiliation wicri:level="2"><nlm:aff id="A3">The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.</nlm:aff><country xml:lang="fr" wicri:curation="lc">États-Unis</country><wicri:regionArea>The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">19251591</idno><idno type="pmc">2758658</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2758658</idno><idno type="RBID">PMC:2758658</idno><idno type="doi">10.1126/science.1171491</idno><date when="2009">2009</date><idno type="wicri:Area/Pmc/Corpus">000529</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000529</idno><idno type="wicri:Area/Pmc/Curation">000529</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000529</idno><idno type="wicri:Area/Pmc/Checkpoint">000C53</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000C53</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Antibody recognition of a highly conserved influenza virus epitope: implications for universal prevention and therapy</title><author><name sortKey="Ekiert, Damian C" sort="Ekiert, Damian C" uniqKey="Ekiert D" first="Damian C." last="Ekiert">Damian C. Ekiert</name><affiliation wicri:level="2"><nlm:aff id="A1">Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.</nlm:aff><country xml:lang="fr" wicri:curation="lc">États-Unis</country><wicri:regionArea>Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author><author><name sortKey="Bhabha, Gira" sort="Bhabha, Gira" uniqKey="Bhabha G" first="Gira" last="Bhabha">Gira Bhabha</name><affiliation wicri:level="2"><nlm:aff id="A1">Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.</nlm:aff><country xml:lang="fr" wicri:curation="lc">États-Unis</country><wicri:regionArea>Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author><author><name sortKey="Elsliger, Marc Andre" sort="Elsliger, Marc Andre" uniqKey="Elsliger M" first="Marc-André" last="Elsliger">Marc-André Elsliger</name><affiliation wicri:level="2"><nlm:aff id="A1">Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.</nlm:aff><country xml:lang="fr" wicri:curation="lc">États-Unis</country><wicri:regionArea>Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author><author><name sortKey="Friesen, Robert H E" sort="Friesen, Robert H E" uniqKey="Friesen R" first="Robert H. E." last="Friesen">Robert H. E. Friesen</name><affiliation wicri:level="1"><nlm:aff id="A2">Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden, The Netherlands</nlm:aff><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden</wicri:regionArea><wicri:noRegion>2301 CA Leiden</wicri:noRegion></affiliation></author><author><name sortKey="Jongeneelen, Mandy" sort="Jongeneelen, Mandy" uniqKey="Jongeneelen M" first="Mandy" last="Jongeneelen">Mandy Jongeneelen</name><affiliation wicri:level="1"><nlm:aff id="A2">Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden, The Netherlands</nlm:aff><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden</wicri:regionArea><wicri:noRegion>2301 CA Leiden</wicri:noRegion></affiliation></author><author><name sortKey="Throsby, Mark" sort="Throsby, Mark" uniqKey="Throsby M" first="Mark" last="Throsby">Mark Throsby</name><affiliation wicri:level="1"><nlm:aff id="A2">Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden, The Netherlands</nlm:aff><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden</wicri:regionArea><wicri:noRegion>2301 CA Leiden</wicri:noRegion></affiliation></author><author><name sortKey="Goudsmit, Jaap" sort="Goudsmit, Jaap" uniqKey="Goudsmit J" first="Jaap" last="Goudsmit">Jaap Goudsmit</name><affiliation wicri:level="1"><nlm:aff id="A2">Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden, The Netherlands</nlm:aff><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Crucell Holland BV, Archimedesweg 4–6, 2301 CA Leiden</wicri:regionArea><wicri:noRegion>2301 CA Leiden</wicri:noRegion></affiliation></author><author><name sortKey="Wilson, Ian A" sort="Wilson, Ian A" uniqKey="Wilson I" first="Ian A." last="Wilson">Ian A. Wilson</name><affiliation wicri:level="2"><nlm:aff id="A1">Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.</nlm:aff><country xml:lang="fr" wicri:curation="lc">États-Unis</country><wicri:regionArea>Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation><affiliation wicri:level="2"><nlm:aff id="A3">The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.</nlm:aff><country xml:lang="fr" wicri:curation="lc">États-Unis</country><wicri:regionArea>The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author></analytic><series><title level="j">Science (New York, N.Y.)</title><idno type="ISSN">0036-8075</idno><idno type="eISSN">1095-9203</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 id="P1">Influenza virus presents a significant and persistent threat to public health worldwide and current vaccines provide immunity to viral isolates similar to the vaccine strain. High affinity antibodies against a conserved epitope could provide immunity to the diverse influenza subtypes and protection against future pandemic viruses. Co-crystal structures were determined at 2.2 and 2.7 Å resolutions for broadly neutralizing human antibody CR6261 Fab in complexes with the major surface antigen (hemagglutinin, HA) from viruses responsible for the 1918 H1N1 influenza pandemic and a recent lethal case of H5N1 avian influenza. In contrast to all other structurally characterized influenza antibodies, CR6261 recognizes a highly conserved helical region in the membrane-proximal stem of HA1/HA2. The antibody neutralizes the virus by blocking conformational rearrangements associated with membrane fusion. The CR6261 epitope identified here should accelerate the design and implementation of improved vaccines that can elicit CR6261-like antibodies, as well as antibody-based therapies for the treatment of influenza.</p></div></front></TEI></pmc><pubmed><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Antibody recognition of a highly conserved influenza virus epitope.</title><author><name sortKey="Ekiert, Damian C" sort="Ekiert, Damian C" uniqKey="Ekiert D" first="Damian C" last="Ekiert">Damian C. Ekiert</name><affiliation wicri:level="2"><nlm:affiliation>Department of Molecular Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author><author><name sortKey="Bhabha, Gira" sort="Bhabha, Gira" uniqKey="Bhabha G" first="Gira" last="Bhabha">Gira Bhabha</name></author><author><name sortKey="Elsliger, Marc Andre" sort="Elsliger, Marc Andre" uniqKey="Elsliger M" first="Marc-André" last="Elsliger">Marc-André Elsliger</name></author><author><name sortKey="Friesen, Robert H E" sort="Friesen, Robert H E" uniqKey="Friesen R" first="Robert H E" last="Friesen">Robert H E. Friesen</name></author><author><name sortKey="Jongeneelen, Mandy" sort="Jongeneelen, Mandy" uniqKey="Jongeneelen M" first="Mandy" last="Jongeneelen">Mandy Jongeneelen</name></author><author><name sortKey="Throsby, Mark" sort="Throsby, Mark" uniqKey="Throsby M" first="Mark" last="Throsby">Mark Throsby</name></author><author><name sortKey="Goudsmit, Jaap" sort="Goudsmit, Jaap" uniqKey="Goudsmit J" first="Jaap" last="Goudsmit">Jaap Goudsmit</name></author><author><name sortKey="Wilson, Ian A" sort="Wilson, Ian A" uniqKey="Wilson I" first="Ian A" last="Wilson">Ian A. Wilson</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:19251591</idno><idno type="pmid">19251591</idno><idno type="doi">10.1126/science.1171491</idno><idno type="wicri:Area/PubMed/Corpus">001802</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001802</idno><idno type="wicri:Area/PubMed/Curation">001802</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001802</idno><idno type="wicri:Area/PubMed/Checkpoint">001677</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001677</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Antibody recognition of a highly conserved influenza virus epitope.</title><author><name sortKey="Ekiert, Damian C" sort="Ekiert, Damian C" uniqKey="Ekiert D" first="Damian C" last="Ekiert">Damian C. Ekiert</name><affiliation wicri:level="2"><nlm:affiliation>Department of Molecular Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author><author><name sortKey="Bhabha, Gira" sort="Bhabha, Gira" uniqKey="Bhabha G" first="Gira" last="Bhabha">Gira Bhabha</name></author><author><name sortKey="Elsliger, Marc Andre" sort="Elsliger, Marc Andre" uniqKey="Elsliger M" first="Marc-André" last="Elsliger">Marc-André Elsliger</name></author><author><name sortKey="Friesen, Robert H E" sort="Friesen, Robert H E" uniqKey="Friesen R" first="Robert H E" last="Friesen">Robert H E. Friesen</name></author><author><name sortKey="Jongeneelen, Mandy" sort="Jongeneelen, Mandy" uniqKey="Jongeneelen M" first="Mandy" last="Jongeneelen">Mandy Jongeneelen</name></author><author><name sortKey="Throsby, Mark" sort="Throsby, Mark" uniqKey="Throsby M" first="Mark" last="Throsby">Mark Throsby</name></author><author><name sortKey="Goudsmit, Jaap" sort="Goudsmit, Jaap" uniqKey="Goudsmit J" first="Jaap" last="Goudsmit">Jaap Goudsmit</name></author><author><name sortKey="Wilson, Ian A" sort="Wilson, Ian A" uniqKey="Wilson I" first="Ian A" last="Wilson">Ian A. Wilson</name></author></analytic><series><title level="j">Science (New York, N.Y.)</title><idno type="eISSN">1095-9203</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antibodies, Viral (chemistry)</term><term>Antibodies, Viral (immunology)</term><term>Antibody Affinity</term><term>Antigens, Viral (chemistry)</term><term>Antigens, Viral (immunology)</term><term>Binding Sites, Antibody</term><term>Crystallization</term><term>Crystallography, X-Ray</term><term>Epitopes (immunology)</term><term>Glycosylation</term><term>Hemagglutinin Glycoproteins, Influenza Virus (chemistry)</term><term>Hemagglutinin Glycoproteins, Influenza Virus (immunology)</term><term>Humans</term><term>Hydrogen Bonding</term><term>Hydrogen-Ion Concentration</term><term>Hydrophobic and Hydrophilic Interactions</term><term>Immunoglobulin Fab Fragments (chemistry)</term><term>Immunoglobulin Fab Fragments (immunology)</term><term>Influenza A Virus, H1N1 Subtype (immunology)</term><term>Influenza A Virus, H5N1 Subtype (immunology)</term><term>Influenza Vaccines</term><term>Membrane Fusion</term><term>Models, Molecular</term><term>Neutralization Tests</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Affinité des anticorps</term><term>Anticorps antiviraux ()</term><term>Anticorps antiviraux (immunologie)</term><term>Antigènes viraux ()</term><term>Antigènes viraux (immunologie)</term><term>Concentration en ions d'hydrogène</term><term>Conformation des protéines</term><term>Cristallisation</term><term>Cristallographie aux rayons X</term><term>Fragments Fab d'immunoglobuline ()</term><term>Fragments Fab d'immunoglobuline (immunologie)</term><term>Fusion membranaire</term><term>Glycoprotéine hémagglutinine du virus influenza ()</term><term>Glycoprotéine hémagglutinine du virus influenza (immunologie)</term><term>Glycosylation</term><term>Humains</term><term>Interactions hydrophobes et hydrophiles</term><term>Liaison hydrogène</term><term>Modèles moléculaires</term><term>Sites de fixation des anticorps</term><term>Sous-type H1N1 du virus de la grippe A (immunologie)</term><term>Sous-type H5N1 du virus de la grippe A (immunologie)</term><term>Structure secondaire des protéines</term><term>Structure tertiaire des protéines</term><term>Tests de neutralisation</term><term>Vaccins antigrippaux</term><term>Épitopes (immunologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antibodies, Viral</term><term>Antigens, Viral</term><term>Hemagglutinin Glycoproteins, Influenza Virus</term><term>Immunoglobulin Fab Fragments</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Viral</term><term>Antigens, Viral</term><term>Epitopes</term><term>Hemagglutinin Glycoproteins, Influenza Virus</term><term>Immunoglobulin Fab Fragments</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Anticorps antiviraux</term><term>Antigènes viraux</term><term>Fragments Fab d'immunoglobuline</term><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Sous-type H1N1 du virus de la grippe A</term><term>Sous-type H5N1 du virus de la grippe A</term><term>Épitopes</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Influenza A Virus, H1N1 Subtype</term><term>Influenza A Virus, H5N1 Subtype</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Antibody Affinity</term><term>Binding Sites, Antibody</term><term>Crystallization</term><term>Crystallography, X-Ray</term><term>Glycosylation</term><term>Humans</term><term>Hydrogen Bonding</term><term>Hydrogen-Ion Concentration</term><term>Hydrophobic and Hydrophilic Interactions</term><term>Influenza Vaccines</term><term>Membrane Fusion</term><term>Models, Molecular</term><term>Neutralization Tests</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Affinité des anticorps</term><term>Anticorps antiviraux</term><term>Antigènes viraux</term><term>Concentration en ions d'hydrogène</term><term>Conformation des protéines</term><term>Cristallisation</term><term>Cristallographie aux rayons X</term><term>Fragments Fab d'immunoglobuline</term><term>Fusion membranaire</term><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Glycosylation</term><term>Humains</term><term>Interactions hydrophobes et hydrophiles</term><term>Liaison hydrogène</term><term>Modèles moléculaires</term><term>Sites de fixation des anticorps</term><term>Structure secondaire des protéines</term><term>Structure tertiaire des protéines</term><term>Tests de neutralisation</term><term>Vaccins antigrippaux</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Influenza virus presents an important and persistent threat to public health worldwide, and current vaccines provide immunity to viral isolates similar to the vaccine strain. High-affinity antibodies against a conserved epitope could provide immunity to the diverse influenza subtypes and protection against future pandemic viruses. Cocrystal structures were determined at 2.2 and 2.7 angstrom resolutions for broadly neutralizing human antibody CR6261 Fab in complexes with the major surface antigen (hemagglutinin, HA) from viruses responsible for the 1918 H1N1 influenza pandemic and a recent lethal case of H5N1 avian influenza. In contrast to other structurally characterized influenza antibodies, CR6261 recognizes a highly conserved helical region in the membrane-proximal stem of HA1 and HA2. The antibody neutralizes the virus by blocking conformational rearrangements associated with membrane fusion. The CR6261 epitope identified here should accelerate the design and implementation of improved vaccines that can elicit CR6261-like antibodies, as well as antibody-based therapies for the treatment of influenza.</div></front></TEI></pubmed></double></record>Pour manipuler ce document sous Unix (Dilib)
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