Distribution of hydrophobic residues is crucial for the fusogenic properties of the Ebola virus GP2 fusion peptide
Distribution of hydrophobic residues is crucial for the fusogenic properties of the Ebola virus GP2 fusion peptide
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DOI：
10.1128/jvi.78.4.2131-2136.2004
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发表时间：
2004-02-01
影响因子：
5.4
通讯作者：
Brasseur, R
中科院分区：
文献类型：
--
作者：
Adam, B;Lins, L;Brasseur, R
研究了埃博拉病毒 GP2 N 末端结构域的脂质不稳定特性。我们的结果表明，埃博拉病毒融合所需的结构域比之前报道的要短。该结构域的融合特性与其在脂质/水界面处的倾斜方向有关，因为螺旋时疏水残基的不对称分布。
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.