Distribution of hydrophobic residues is crucial for the fusogenic properties of the Ebola virus GP2 fusion peptide.
The lipid-destabilizing properties of the N-terminal domain of the GP2 of Ebola virus were investigated. Our results suggest that the domain of Ebola virus needed for fusion is shorter than that previously reported. The fusogenic properties of this domain are related to its oblique orientation at the lipid/water interface owing to an asymmetric distribution of the hydrophobic residues when helical.
Adam
B
B
Centre de Biophysique Moléculaire Numérique, FSAGX, 5030 Gembloux, Leuven, Belgium.
Lins
L
L
Stroobant
V
V
Thomas
A
A
Brasseur
R
R
D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D029043:Ebolavirus / Q000472:pathogenicity*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008051:Lipid Bilayers; D008081:Liposomes / Q000737:chemistry; D008561:Membrane Fusion; D008566:Membranes / Q000737:chemistry; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000378:metabolism*
D000596:Amino Acids; D008051:Lipid Bilayers; D008081:Liposomes; D010455:Peptides; D014759:Viral Envelope Proteins