Structure of influenza haemagglutinin at neutral and at fusogenic pH by electron cryo-microscopy.
Identifieur interne : 000012 ( Ncbi/Checkpoint ); précédent : 000011; suivant : 000013Structure of influenza haemagglutinin at neutral and at fusogenic pH by electron cryo-microscopy.
Auteurs : C. Böttcher [Allemagne] ; K. Ludwig ; A. Herrmann ; M. Van Heel ; H. StarkSource :
- 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.
- Cryoelectron Microscopy, Hydrogen-Ion Concentration, Models, Molecular, Protein Conformation.
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 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.
DOI: 10.1016/s0014-5793(99)01475-1
PubMed: 10606732
Affiliations:
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pubmed:10606732Le document en format XML
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<term>Hydrogen-Ion Concentration</term>
<term>Influenza A virus (chemistry)</term>
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<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>
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