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An architecture for the fusion site of Influenza hemagglutinin
Journal article   Open access   Peer reviewed

An architecture for the fusion site of Influenza hemagglutinin

Joe Bentz, Harma Ellens and Dennis Alford
FEBS letters, v 276(1), pp 1-5
1990
PMID: 2265687
url
https://doi.org/10.1016/0014-5793(90)80492-2View
Published, Version of Record (VoR)Maybe Open Access (Publisher Bronze) Open

Abstract

Envelope glycoprotein Fusion protein Influenza hemagglutinin Lipid-protein interaction Liposome Membrane fusion
The recent finding that more than one Influenza hemagglutinin (HA) is required at the fusion site for HA-expressing fibroblasts [1], together with the crystal structure of HA at neutral pH [2], provide the basic elements of a plausible model for this fusion site. Within an aggregate of HA trimers at low pH, we propose fusion intermediates which are based upon a minimal alteration to the known neutral pH structure of HA and which should have reasonable activation energies. This is the first model of a glycoprotein-mediated fusion site which explicitly accounts for the disposition of the lipids within these intermediates. While the fusion site created by HA will not be the same as that of eukaryotic fusion complexes [3], general characteristics could be shared.

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Collaboration types
Industry collaboration
Domestic collaboration
Web of Science research areas
Biochemistry & Molecular Biology
Biophysics
Cell Biology
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