Distribution of hydrophobic residues is crucial for the fusogenic properties of the Ebola virus GP2 fusion peptide

被引：25

作者：

Adam, B

Lins, L

Stroobant, V

Thomas, A

Brasseur, R

机构：

[1] FSAGX, Ctr Biophys Mol Numer, B-5030 Gembloux, Belgium

[2] UCL, Ludwig Inst, Louvain, Belgium

来源：

JOURNAL OF VIROLOGY | 2004年 / 78卷 / 04期

关键词：

D O I：

10.1128/JVI.78.4.2131-2136.2004

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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.

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页码：2131 / 2136

页数：6

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