Analyzing the fusion process of influenza hemagglutinin by mutagenesis and molecular modeling
Biophysical JournalPublished 1 April 1992Open access
H. Robert Guy, Stewart R. Durell, Christian Schoch, Robert Blumenthal
Citations34
SJR quartileQ1
SJR score1.11
SNIP0.82
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TL;DR
Computer graphics and computational chemistry methods are used to develop plausible models for how Hemagglutinin may change conformations and associate with adjacent HA trimers during the fusion process.
Keywords
MedicineBiochemistry, Genetics and Molecular Biology
NatureStructure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
2,530 Citations1981Ian A. Wilson, J.J. Skehel +1 more
The haemagglutinin glycoprotein of influenza virus is a trimer comprising two structurally distinct regions: a triple-stranded coiled-coil of α-helices extends 76 Å from the membrane and a globular region of antiparallel β-sheet is positioned on top of this stem.
The Journal of Cell BiologyStudies on the mechanism of membrane fusion: site-specific mutagenesis of the hemagglutinin of influenza virus.
341 Citations1986M J Gething, Robert W. Doms +2 more
A mutant protein was constructed that induced fusion of erythrocytes with cells with the same efficiency and pH profile as the wild-type protein, and the ability of this mutant to induce polykaryon formation was greatly impaired.
The EMBO JournalIntermediates in influenza induced membrane fusion.
246 Citations1990Thomas Stegmann, Judith M. White +1 more
The results show that the mechanism by which influenza virus fuses with target membranes involves sequential complex changes in the hemagglutinin (HA, the viral fusion protein) and in the contact site between virus and target membrane and leads to a revised model for HA mediated fusion.
Journal of Biological ChemistryKinetics of pH-dependent fusion between 3T3 fibroblasts expressing influenza hemagglutinin and red blood cells
149 Citations1989Stephen J. Morris, Debi P. Sarkar +2 more
Analysis of the data indicates that the pH-induced membrane fusion activity of HA is a highly cooperative event.
NaturePatch clamp studies of single cell-fusion events mediated by a viral fusion protein
148 Citations1989Austen Spruce, Atsushi Iwata +2 more
It is suggested that, as in exocytosis5, HA-mediated membrane fusion begins with the formation of a narrow pore, and the initial diameter of the pore is estimated to be no more than twice that of a gap junction channel.
Journal of VirologyQuaternary structure of influenza virus hemagglutinin after acid treatment
138 Citations1986Robert W. Doms, Ari Helenius
Negative-stain electron microscopy supported the notion that HA molecules in virus particles do not dissociate upon acidification and may form larger oligomeric structures in the plane of the viral membrane and the role of the transmembrane anchors of HA in preventing dissociation of the trimer.
The Journal of Cell BiologyInitial stages of influenza hemagglutinin-induced cell fusion monitored simultaneously by two fluorescent events: cytoplasmic continuity and lipid mixing.
118 Citations1989Debi P. Sarkar, Stephen J. Morris +3 more
The kinetics, pH profile, and temperature dependence were similar for both fluorescent events measured simultaneously, indicating that influenza hemagglutinin-induced fusion rapidly establishes bilayer continuity and exchange of cytoplasmic contents.
FEBS LettersAn architecture for the fusion site of Influenza hemagglutinin
92 Citations1990Joe Bentz, Harma Ellens +1 more
This is the first model of a glycoprotein‐mediated fusion site which explicitly accounts for the disposition of the lipids within these intermediates and the fusion site created by HA will not be the same as that of eukaryotic fusion complexes.
Journal of Molecular BiologyElectron microscopy of influenza virus
83 Citations1985Frank P. Booy, Rob W. H. Ruigrok +1 more
It is shown that cryo-electron microscopy confirms and extends the data obtained by conventional methods of electron microscopical study of the influenza virus, type B/Hong Kong, in the unstained, frozen, hydrated state after quench-freezing in cooled liquid ethane.
