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Structure of influenza haemagglutinin at neutral and at fusogenic pH by electron cryo-microscopy

Identifieur interne : 001987 ( Main/Exploration ); précédent : 001986; suivant : 001988

Structure 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 :

RBID : ISTEX:2E44183DE2006E8235FC42EB2D04C37014438D4A

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English descriptors

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


Affiliations:


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<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>
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<term>Concentration en ions d'hydrogène</term>
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<term>Cryomicroscopie électronique</term>
<term>Hémagglutinines virales ()</term>
<term>Hémagglutinines virales (ultrastructure)</term>
<term>Modèles moléculaires</term>
<term>Virus de la grippe A ()</term>
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<term>Angular approach</term>
<term>Angular reconstitution</term>
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<term>Cell biol</term>
<term>Central cavity</term>
<term>Cold spring harb</term>
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<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 capacity</term>
<term>Fusion peptide</term>
<term>Fusion sequence</term>
<term>Geel zwart</term>
<term>Haemagglutinin</term>
<term>Haemagglutinin trimer</term>
<term>Hydrogen-Ion Concentration</term>
<term>Image processing procedure</term>
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<term>Micrographs</term>
<term>Models, Molecular</term>
<term>Projection images</term>
<term>Protein Conformation</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>
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<term>Cryomicroscopie électronique</term>
<term>Hémagglutinines virales</term>
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<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>
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