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X‐ray diffraction study of feline leukemia virus fusion peptide and lipid polymorphism
Author(s) -
Darkes Malcolm J.M,
Davies Sarah M.A,
Bradshaw Jeremy P
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)01454-4
Subject(s) - peptide , lipid bilayer fusion , feline leukemia virus , biophysics , phospholipid , membrane , fusion , crystallography , membrane curvature , chemistry , lipid bilayer , biology , biochemistry , virus , virology , linguistics , philosophy
The structural effects of the fusion peptide of feline leukemia virus (FeLV) on the lipid polymorphism of N ‐methylated dioleoylphosphatidylethanolamine were studied using a temperature ramp with sequential X‐ray diffraction. This peptide, the hydrophobic amino‐terminus of p15E, has been proven to be fusogenic and to promote the formation of highly curved, intermediate structures on the lamellar liquid‐crystal to inverse hexagonal phase transition pathway. The FeLV peptide produces marked effects on the thermotropic mesomorphic behaviour of MeDOPE, a phospholipid with an intermediate spontaneous radius of curvature. The peptide is shown to reduce the lamellar repeat distance of the membrane prior to the onset of an inverted cubic phase. This suggests that membrane thinning may play a role in peptide‐induced membrane fusion and strengthens the link between the fusion pathway and inverted cubic phase formation. The results of this study are interpreted in relation to models of the membrane fusion mechanism.