Structure of influenza haemagglutinin at neutral and at fusogenic pH by electron cryo-microscopy
Identifieur interne : 000220 ( Istex/Curation ); précédent : 000219; suivant : 000221Structure 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.
English descriptors
- Teeft :
- Acidic, Angular approach, Angular reconstitution, Biol, Cell biol, Central cavity, Cold spring harb, Conformation, Conformational, Conformational change, Conformational states, Conformational transitions, 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, Image processing procedure, Individual trimers, Loop region, Membrane, Micrographs, Projection images, 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
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: Pour aller vers cette notice dans l'étape Curation :000220
Links to Exploration step
ISTEX:2E44183DE2006E8235FC42EB2D04C37014438D4ALe document en format XML
<record><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>
<affiliation wicri:level="1"><mods:affiliation>Freie Universität Berlin, Institut für Chemie/Forschungszentrum für Elektronenmikroskopie, Fabeckstr. 36a, D-14195 Berlin, Germany</mods: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>
</affiliation>
</author>
<author><name sortKey="Ludwig, Kai" sort="Ludwig, Kai" uniqKey="Ludwig K" first="Kai" last="Ludwig">Kai Ludwig</name>
<affiliation wicri:level="1"><mods:affiliation>Humboldt-Universität zu Berlin, Math.-Nat. Fak. I, Institut für Biologie/Biophysik, Invalidenstr. 43, D-10115 Berlin, Germany</mods:affiliation>
<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>
</affiliation>
</author>
<author><name sortKey="Herrmann, Andreas" sort="Herrmann, Andreas" uniqKey="Herrmann A" first="Andreas" last="Herrmann">Andreas Herrmann</name>
<affiliation wicri:level="1"><mods:affiliation>Humboldt-Universität zu Berlin, Math.-Nat. Fak. I, Institut für Biologie/Biophysik, Invalidenstr. 43, D-10115 Berlin, Germany</mods:affiliation>
<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>
</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"><mods:affiliation>Imperial College of Science, Medicine and Technology, Wolfson Laboratories, Department of Biochemistry, London SW7 2AY, UK</mods:affiliation>
<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>
</affiliation>
</author>
<author><name sortKey="Stark, Holger" sort="Stark, Holger" uniqKey="Stark H" first="Holger" last="Stark">Holger Stark</name>
<affiliation wicri:level="1"><mods:affiliation>Fritz-Haber-Institut, Max-Planck-Gesellschaft, Faradayweg 4-6, D-14195 Berlin, Germany</mods:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Fritz-Haber-Institut, Max-Planck-Gesellschaft, Faradayweg 4-6, D-14195 Berlin</wicri:regionArea>
</affiliation>
<affiliation wicri:level="1"><mods:affiliation>Institut für Molekularbiologie und Tumorforschung, Emil-Mannkopff-Strasse 2, D-35037 Marburg, Germany</mods:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Institut für Molekularbiologie und Tumorforschung, Emil-Mannkopff-Strasse 2, D-35037 Marburg</wicri:regionArea>
</affiliation>
<affiliation><mods:affiliation>Corresponding author. Fax: (49)-6421-286 7008</mods:affiliation>
<wicri:noCountry code="no comma">Corresponding author. Fax: (49)-6421-286 7008</wicri:noCountry>
</affiliation>
<affiliation wicri:level="1"><mods:affiliation>E-mail: stark@imt.uni-marburg.de</mods:affiliation>
<country wicri:rule="url">Allemagne</country>
</affiliation>
</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>
</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="1"><mods:affiliation>Freie Universität Berlin, Institut für Chemie/Forschungszentrum für Elektronenmikroskopie, Fabeckstr. 36a, D-14195 Berlin, Germany</mods: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>
</affiliation>
</author>
<author><name sortKey="Ludwig, Kai" sort="Ludwig, Kai" uniqKey="Ludwig K" first="Kai" last="Ludwig">Kai Ludwig</name>
<affiliation wicri:level="1"><mods:affiliation>Humboldt-Universität zu Berlin, Math.-Nat. Fak. I, Institut für Biologie/Biophysik, Invalidenstr. 43, D-10115 Berlin, Germany</mods:affiliation>
<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>
</affiliation>
</author>
<author><name sortKey="Herrmann, Andreas" sort="Herrmann, Andreas" uniqKey="Herrmann A" first="Andreas" last="Herrmann">Andreas Herrmann</name>
<affiliation wicri:level="1"><mods:affiliation>Humboldt-Universität zu Berlin, Math.-Nat. Fak. I, Institut für Biologie/Biophysik, Invalidenstr. 43, D-10115 Berlin, Germany</mods:affiliation>
<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>
</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"><mods:affiliation>Imperial College of Science, Medicine and Technology, Wolfson Laboratories, Department of Biochemistry, London SW7 2AY, UK</mods:affiliation>
<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>
</affiliation>
</author>
<author><name sortKey="Stark, Holger" sort="Stark, Holger" uniqKey="Stark H" first="Holger" last="Stark">Holger Stark</name>
<affiliation wicri:level="1"><mods:affiliation>Fritz-Haber-Institut, Max-Planck-Gesellschaft, Faradayweg 4-6, D-14195 Berlin, Germany</mods:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Fritz-Haber-Institut, Max-Planck-Gesellschaft, Faradayweg 4-6, D-14195 Berlin</wicri:regionArea>
</affiliation>
<affiliation wicri:level="1"><mods:affiliation>Institut für Molekularbiologie und Tumorforschung, Emil-Mannkopff-Strasse 2, D-35037 Marburg, Germany</mods:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Institut für Molekularbiologie und Tumorforschung, Emil-Mannkopff-Strasse 2, D-35037 Marburg</wicri:regionArea>
</affiliation>
<affiliation><mods:affiliation>Corresponding author. Fax: (49)-6421-286 7008</mods:affiliation>
</affiliation>
<affiliation wicri:level="1"><mods:affiliation>E-mail: stark@imt.uni-marburg.de</mods:affiliation>
<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>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/H2N2V1/Data/Istex/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000220 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Istex/Curation/biblio.hfd -nk 000220 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= H2N2V1 |flux= Istex |étape= Curation |type= RBID |clé= ISTEX:2E44183DE2006E8235FC42EB2D04C37014438D4A |texte= Structure of influenza haemagglutinin at neutral and at fusogenic pH by electron cryo-microscopy }}
This area was generated with Dilib version V0.6.33. |