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Testing topological models for the membrane penetration of the fusion peptide of influenza virus hemagglutinin
Author(s) -
Brunner Josef
Publication year - 1989
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 - 10.1016/0014-5793(89)81574-1
Subject(s) - hemagglutinin (influenza) , penetration (warfare) , virus , virology , peptide , fusion , lipid bilayer fusion , membrane , influenza a virus , chemistry , biophysics , biology , biochemistry , mathematics , linguistics , philosophy , operations research
Low pH‐induced binding of the bromelain‐solubilized form of influenza virus hemagglutinin (BHA) to membranes occurs through the fusion peptide. From asymmetric hydrophobic photolabeling of membranes, evidence was obtained that this peptide penetrates only one leaflet of the bilayer. The asymmetrical labeling was achieved by employing a photoreactive analogue of a fatty acid whose transbilayer distribution can be manipulated by a membrane proton gradient.