Structure of influenza haemagglutinin at neutral and at fusogenic pH by electron cryo-microscopy
Identifieur interne : 001987 ( Main/Curation ); précédent : 001986; suivant : 001988Structure of influenza haemagglutinin at neutral and at fusogenic pH by electron cryo-microscopy
Auteurs : Christoph Böttcher [Allemagne] ; Kai Ludwig [Allemagne] ; Andreas Herrmann [Allemagne] ; Marin Van Heel [Royaume-Uni] ; Holger Stark [Allemagne]Source :
- FEBS Letters [ 0014-5793 ] ; 1999.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Hemagglutinins, Viral.
- chemical , ultrastructure : Hemagglutinins, Viral.
- chemistry : Influenza A virus.
- Teeft :
- Acidic, Angular approach, Angular reconstitution, Biol, Cell biol, Central cavity, Cold spring harb, Conformation, Conformational, Conformational change, Conformational states, Conformational transitions, Cryoelectron Microscopy, Crystallographic structure, Digitised micrographs, Distal domains, Ectodomain, Entire ectodomain, Feb, Fourier shell correlation, Fourier space, Fusion capacity, Fusion peptide, Fusion sequence, Geel zwart, Haemagglutinin, Haemagglutinin trimer, Hydrogen-Ion Concentration, Image processing procedure, Individual trimers, Loop region, Membrane, Micrographs, Models, Molecular, Projection images, Protein Conformation, Rosette, Skehel, Subunit, Target membrane, Target membranes, Trimer, Trimeric ectodomain, Viral, Viral membrane, Whole trimer.
Abstract
Abstract: The three-dimensional structures of the complete haemagglutinin (HA) of influenza virus A/Japan/305/57 (H2N2) in its native (neutral pH) and membrane fusion-competent (low pH) form by electron cryo-microscopy at a resolution of 10 Å and 14 Å, respectively, have been determined. In the fusion-competent form the subunits remain closely associated preserving typical overall features of the trimeric ectodomain at neutral pH. Rearrangements of the tertiary structure in the distal and the stem parts are associated with the formation of a central cavity through the entire ectodomain. We suggest that the cavity is essential for relocation of the so-called fusion sequence of HA towards the target membrane.
Url:
DOI: 10.1016/S0014-5793(99)01475-1
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scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Hemagglutinins, Viral</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Influenza A virus</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Hémagglutinines virales</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Acidic</term><term>Angular approach</term><term>Angular reconstitution</term><term>Biol</term><term>Cell biol</term><term>Central cavity</term><term>Cold spring harb</term><term>Conformation</term><term>Conformational</term><term>Conformational change</term><term>Conformational states</term><term>Conformational transitions</term><term>Cryoelectron Microscopy</term><term>Crystallographic structure</term><term>Digitised micrographs</term><term>Distal domains</term><term>Ectodomain</term><term>Entire ectodomain</term><term>Feb</term><term>Fourier shell correlation</term><term>Fourier space</term><term>Fusion 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ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The three-dimensional structures of the complete haemagglutinin (HA) of influenza virus A/Japan/305/57 (H2N2) in its native (neutral pH) and membrane fusion-competent (low pH) form by electron cryo-microscopy at a resolution of 10 Å and 14 Å, respectively, have been determined. In the fusion-competent form the subunits remain closely associated preserving typical overall features of the trimeric ectodomain at neutral pH. Rearrangements of the tertiary structure in the distal and the stem parts are associated with the formation of a central cavity through the entire ectodomain. We suggest that the cavity is essential for relocation of the so-called fusion sequence of HA towards the target membrane.</div></front></TEI><double idat="0014-5793:1999:Bottcher C:structure:of:influenza"><ISTEX><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>Structure of influenza haemagglutinin at neutral and at fusogenic pH by electron cryo-microscopy</title><author><name sortKey="Bottcher, Christoph" sort="Bottcher, Christoph" uniqKey="Bottcher C" first="Christoph" last="Böttcher">Christoph Böttcher</name></author><author><name sortKey="Ludwig, Kai" sort="Ludwig, Kai" uniqKey="Ludwig K" first="Kai" last="Ludwig">Kai Ludwig</name></author><author><name sortKey="Herrmann, Andreas" sort="Herrmann, Andreas" uniqKey="Herrmann A" first="Andreas" last="Herrmann">Andreas Herrmann</name></author><author><name sortKey="Van Heel, Marin" sort="Van Heel, Marin" uniqKey="Van Heel M" first="Marin" last="Van Heel">Marin Van Heel</name></author><author><name sortKey="Stark, Holger" sort="Stark, Holger" uniqKey="Stark H" first="Holger" last="Stark">Holger Stark</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:2E44183DE2006E8235FC42EB2D04C37014438D4A</idno><date when="1999" year="1999">1999</date><idno type="doi">10.1016/S0014-5793(99)01475-1</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-PCN76582-4/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000220</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000220</idno><idno type="wicri:Area/Istex/Curation">000220</idno><idno type="wicri:Area/Istex/Checkpoint">000787</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">000787</idno><idno type="wicri:doubleKey">0014-5793:1999:Bottcher C:structure:of:influenza</idno><idno type="wicri:Area/Main/Merge">001A34</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Structure of influenza haemagglutinin at neutral and at fusogenic pH by electron cryo-microscopy</title><author><name sortKey="Bottcher, Christoph" sort="Bottcher, Christoph" uniqKey="Bottcher C" first="Christoph" last="Böttcher">Christoph Böttcher</name><affiliation wicri:level="3"><country xml:lang="fr">Allemagne</country><wicri:regionArea>Freie Universität Berlin, Institut für Chemie/Forschungszentrum für Elektronenmikroskopie, Fabeckstr. 36a, D-14195 Berlin</wicri:regionArea><placeName><region type="land" nuts="3">Berlin</region><settlement type="city">Berlin</settlement></placeName></affiliation></author><author><name sortKey="Ludwig, Kai" sort="Ludwig, Kai" uniqKey="Ludwig K" first="Kai" last="Ludwig">Kai Ludwig</name><affiliation wicri:level="3"><country xml:lang="fr">Allemagne</country><wicri:regionArea>Humboldt-Universität zu Berlin, Math.-Nat. Fak. I, Institut für Biologie/Biophysik, Invalidenstr. 43, D-10115 Berlin</wicri:regionArea><placeName><region type="land" nuts="3">Berlin</region><settlement type="city">Berlin</settlement></placeName></affiliation></author><author><name sortKey="Herrmann, Andreas" sort="Herrmann, Andreas" uniqKey="Herrmann A" first="Andreas" last="Herrmann">Andreas Herrmann</name><affiliation wicri:level="3"><country xml:lang="fr">Allemagne</country><wicri:regionArea>Humboldt-Universität zu Berlin, Math.-Nat. Fak. I, Institut für Biologie/Biophysik, Invalidenstr. 43, D-10115 Berlin</wicri:regionArea><placeName><region type="land" nuts="3">Berlin</region><settlement type="city">Berlin</settlement></placeName></affiliation></author><author><name sortKey="Van Heel, Marin" sort="Van Heel, Marin" uniqKey="Van Heel M" first="Marin" last="Van Heel">Marin Van Heel</name><affiliation wicri:level="1"><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Imperial College of Science, Medicine and Technology, Wolfson Laboratories, Department of Biochemistry, London SW7 2AY</wicri:regionArea><wicri:noRegion>London SW7 2AY</wicri:noRegion></affiliation></author><author><name sortKey="Stark, Holger" sort="Stark, Holger" uniqKey="Stark H" first="Holger" last="Stark">Holger Stark</name><affiliation wicri:level="3"><country xml:lang="fr">Allemagne</country><wicri:regionArea>Fritz-Haber-Institut, Max-Planck-Gesellschaft, Faradayweg 4-6, D-14195 Berlin</wicri:regionArea><placeName><region type="land" nuts="3">Berlin</region><settlement type="city">Berlin</settlement></placeName></affiliation><affiliation wicri:level="3"><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Molekularbiologie und Tumorforschung, Emil-Mannkopff-Strasse 2, D-35037 Marburg</wicri:regionArea><placeName><region type="land" nuts="1">Hesse (Land)</region><region type="district" nuts="2">District de Giessen</region><settlement type="city">Marbourg</settlement></placeName></affiliation><affiliation></affiliation><affiliation wicri:level="1"><country wicri:rule="url">Allemagne</country></affiliation></author></analytic><monogr></monogr><series><title level="j">FEBS Letters</title><title level="j" type="abbrev">FEBS</title><idno type="ISSN">0014-5793</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1999">1999</date><biblScope unit="volume">463</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="255">255</biblScope><biblScope unit="page" to="259">259</biblScope></imprint><idno type="ISSN">0014-5793</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0014-5793</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acidic</term><term>Angular approach</term><term>Angular reconstitution</term><term>Biol</term><term>Cell biol</term><term>Central cavity</term><term>Cold spring harb</term><term>Conformation</term><term>Conformational</term><term>Conformational change</term><term>Conformational states</term><term>Conformational transitions</term><term>Crystallographic structure</term><term>Digitised micrographs</term><term>Distal domains</term><term>Ectodomain</term><term>Entire ectodomain</term><term>Feb</term><term>Fourier shell correlation</term><term>Fourier space</term><term>Fusion capacity</term><term>Fusion peptide</term><term>Fusion sequence</term><term>Geel zwart</term><term>Haemagglutinin</term><term>Haemagglutinin trimer</term><term>Image processing procedure</term><term>Individual trimers</term><term>Loop region</term><term>Membrane</term><term>Micrographs</term><term>Projection images</term><term>Rosette</term><term>Skehel</term><term>Subunit</term><term>Target membrane</term><term>Target membranes</term><term>Trimer</term><term>Trimeric ectodomain</term><term>Viral</term><term>Viral membrane</term><term>Whole trimer</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The three-dimensional structures of the complete haemagglutinin (HA) of influenza virus A/Japan/305/57 (H2N2) in its native (neutral pH) and membrane fusion-competent (low pH) form by electron cryo-microscopy at a resolution of 10 Å and 14 Å, respectively, have been determined. In the fusion-competent form the subunits remain closely associated preserving typical overall features of the trimeric ectodomain at neutral pH. Rearrangements of the tertiary structure in the distal and the stem parts are associated with the formation of a central cavity through the entire ectodomain. We suggest that the cavity is essential for relocation of the so-called fusion sequence of HA towards the target membrane.</div></front></TEI></ISTEX><PubMed><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Structure of influenza haemagglutinin at neutral and at fusogenic pH by electron cryo-microscopy.</title><author><name sortKey="Bottcher, C" sort="Bottcher, C" uniqKey="Bottcher C" first="C" last="Böttcher">C. Böttcher</name><affiliation wicri:level="3"><nlm:affiliation>Freie Universität Berlin, Institut für Chemie/Forschungszentrum für Elektronenmikroskopie, Fabeckstr. 36a, D-14195, Berlin, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Freie Universität Berlin, Institut für Chemie/Forschungszentrum für Elektronenmikroskopie, Fabeckstr. 36a, D-14195, Berlin</wicri:regionArea><placeName><region type="land" nuts="3">Berlin</region><settlement type="city">Berlin</settlement></placeName></affiliation></author><author><name sortKey="Ludwig, K" sort="Ludwig, K" uniqKey="Ludwig K" first="K" last="Ludwig">K. Ludwig</name></author><author><name sortKey="Herrmann, A" sort="Herrmann, A" uniqKey="Herrmann A" first="A" last="Herrmann">A. Herrmann</name></author><author><name sortKey="Van Heel, M" sort="Van Heel, M" uniqKey="Van Heel M" first="M" last="Van Heel">M. 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Böttcher</name><affiliation wicri:level="3"><nlm:affiliation>Freie Universität Berlin, Institut für Chemie/Forschungszentrum für Elektronenmikroskopie, Fabeckstr. 36a, D-14195, Berlin, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Freie Universität Berlin, Institut für Chemie/Forschungszentrum für Elektronenmikroskopie, Fabeckstr. 36a, D-14195, Berlin</wicri:regionArea><placeName><region type="land" nuts="3">Berlin</region><settlement type="city">Berlin</settlement></placeName></affiliation></author><author><name sortKey="Ludwig, K" sort="Ludwig, K" uniqKey="Ludwig K" first="K" last="Ludwig">K. Ludwig</name></author><author><name sortKey="Herrmann, A" sort="Herrmann, A" uniqKey="Herrmann A" first="A" last="Herrmann">A. Herrmann</name></author><author><name sortKey="Van Heel, M" sort="Van Heel, M" uniqKey="Van Heel M" first="M" last="Van Heel">M. Van Heel</name></author><author><name sortKey="Stark, H" sort="Stark, H" uniqKey="Stark H" first="H" last="Stark">H. Stark</name></author></analytic><series><title level="j">FEBS letters</title><idno type="ISSN">0014-5793</idno><imprint><date when="1999" type="published">1999</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cryoelectron Microscopy</term><term>Hemagglutinins, Viral (chemistry)</term><term>Hemagglutinins, Viral (ultrastructure)</term><term>Hydrogen-Ion Concentration</term><term>Influenza A virus (chemistry)</term><term>Models, Molecular</term><term>Protein Conformation</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Concentration en ions d'hydrogène</term><term>Conformation des protéines</term><term>Cryomicroscopie électronique</term><term>Hémagglutinines virales ()</term><term>Hémagglutinines virales (ultrastructure)</term><term>Modèles moléculaires</term><term>Virus de la grippe A ()</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Hemagglutinins, Viral</term></keywords><keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Hemagglutinins, Viral</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Influenza A virus</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Hémagglutinines virales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cryoelectron Microscopy</term><term>Hydrogen-Ion Concentration</term><term>Models, Molecular</term><term>Protein Conformation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Concentration en ions d'hydrogène</term><term>Conformation des protéines</term><term>Cryomicroscopie électronique</term><term>Hémagglutinines virales</term><term>Modèles moléculaires</term><term>Virus de la grippe A</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The three-dimensional structures of the complete haemagglutinin (HA) of influenza virus A/Japan/305/57 (H2N2) in its native (neutral pH) and membrane fusion-competent (low pH) form by electron cryo-microscopy at a resolution of 10 A and 14 A, respectively, have been determined. In the fusion-competent form the subunits remain closely associated preserving typical overall features of the trimeric ectodomain at neutral pH. Rearrangements of the tertiary structure in the distal and the stem parts are associated with the formation of a central cavity through the entire ectodomain. We suggest that the cavity is essential for relocation of the so-called fusion sequence of HA towards the target membrane.</div></front></TEI></PubMed></double></record>Pour manipuler ce document sous Unix (Dilib)
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