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Structure of influenza haemagglutinin at neutral and at fusogenic pH by electron cryo‐microscopy
Author(s) -
Böttcher Christoph,
Ludwig Kai,
Herrmann Andreas,
van Heel Marin,
Stark Holger
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01475-1
Subject(s) - ectodomain , lipid bilayer fusion , cryo electron microscopy , electron microscope , biophysics , fusion , chemistry , crystallography , membrane , resolution (logic) , biology , biochemistry , physics , optics , receptor , linguistics , philosophy , artificial intelligence , computer science
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.