Antibody recognition of a highly conserved influenza virus epitope.
Identifieur interne : 001677 ( PubMed/Checkpoint ); précédent : 001676; suivant : 001678Antibody recognition of a highly conserved influenza virus epitope.
Auteurs : Damian C. Ekiert [États-Unis] ; Gira Bhabha ; Marc-André Elsliger ; Robert H E. Friesen ; Mandy Jongeneelen ; Mark Throsby ; Jaap Goudsmit ; Ian A. WilsonSource :
- Science (New York, N.Y.) [ 1095-9203 ] ; 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 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.
DOI: 10.1126/science.1171491
PubMed: 19251591
Affiliations:
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pubmed:19251591Le document en format XML
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(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><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19251591</PMID><DateCompleted><Year>2009</Year><Month>05</Month><Day>01</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1095-9203</ISSN><JournalIssue CitedMedium="Internet"><Volume>324</Volume><Issue>5924</Issue><PubDate><Year>2009</Year><Month>Apr</Month><Day>10</Day></PubDate></JournalIssue><Title>Science (New York, N.Y.)</Title><ISOAbbreviation>Science</ISOAbbreviation></Journal><ArticleTitle>Antibody recognition of a highly conserved influenza virus epitope.</ArticleTitle><Pagination><MedlinePgn>246-51</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1126/science.1171491</ELocationID><Abstract><AbstractText>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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ekiert</LastName><ForeName>Damian C</ForeName><Initials>DC</Initials><AffiliationInfo><Affiliation>Department of Molecular Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bhabha</LastName><ForeName>Gira</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Elsliger</LastName><ForeName>Marc-André</ForeName><Initials>MA</Initials></Author><Author ValidYN="Y"><LastName>Friesen</LastName><ForeName>Robert H E</ForeName><Initials>RH</Initials></Author><Author ValidYN="Y"><LastName>Jongeneelen</LastName><ForeName>Mandy</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Throsby</LastName><ForeName>Mark</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Goudsmit</LastName><ForeName>Jaap</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Wilson</LastName><ForeName>Ian A</ForeName><Initials>IA</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>3GBM</AccessionNumber><AccessionNumber>3GBN</AccessionNumber></AccessionNumberList></DataBank></DataBankList><GrantList CompleteYN="Y"><Grant><GrantID>Y1-GM-1104</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>U54 GM074898-03</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>AI-058113</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>U54 GM074898</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>Y1-CO-1020</GrantID><Acronym>CO</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>P01 AI058113-040002</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>P01 AI058113</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2009</Year><Month>02</Month><Day>26</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Science</MedlineTA><NlmUniqueID>0404511</NlmUniqueID><ISSNLinking>0036-8075</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000914">Antibodies, Viral</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000956">Antigens, Viral</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000939">Epitopes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019267">Hemagglutinin Glycoproteins, Influenza Virus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007140">Immunoglobulin Fab Fragments</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007252">Influenza Vaccines</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C109963">hemagglutinin, avian influenza A virus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C483468">hemagglutinin, human influenza A virus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000914" MajorTopicYN="N">Antibodies, Viral</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000915" MajorTopicYN="Y">Antibody Affinity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000956" MajorTopicYN="N">Antigens, Viral</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001666" MajorTopicYN="Y">Binding Sites, Antibody</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003460" MajorTopicYN="N">Crystallization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000939" MajorTopicYN="N">Epitopes</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006031" MajorTopicYN="N">Glycosylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019267" MajorTopicYN="N">Hemagglutinin Glycoproteins, Influenza Virus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006860" MajorTopicYN="N">Hydrogen Bonding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D057927" MajorTopicYN="N">Hydrophobic and Hydrophilic Interactions</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007140" MajorTopicYN="N">Immunoglobulin Fab Fragments</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D053118" MajorTopicYN="N">Influenza A Virus, H1N1 Subtype</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D053124" MajorTopicYN="N">Influenza A Virus, H5N1 Subtype</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007252" MajorTopicYN="N">Influenza Vaccines</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008561" MajorTopicYN="N">Membrane Fusion</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009500" MajorTopicYN="N">Neutralization Tests</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate 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