The central structural feature of the membrane fusion protein subunit from the Ebola virus glycoprotein is a long triple-stranded coiled coil
The central structural feature of the membrane fusion protein subunit from the Ebola virus glycoprotein is a long triple-stranded coiled coil
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DOI：
10.1073/pnas.95.11.6032
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发表时间：
1998-05-26
影响因子：
11.1
通讯作者：
Wiley, DC
中科院分区：
文献类型：
--
作者：
Weissenhorn, W;Calder, LJ;Wiley, DC
埃博拉病毒Gp2糖蛋白的外结构域被来自GCN4 （pIIGCN4）的三聚异亮氨酸拉链溶解，取代了N端疏水融合肽。通过化学交联和圆二色性，这种嵌合分子形成了三聚体，具有高度的α -螺旋和非常耐热性的分子。电镜显示，Gp2折叠成类似于流感病毒HA2和HIV-1 gp41的杆状结构，进一步证明了来自正粘病毒科（流感）、逆转录病毒科（HIV-1）和丝状病毒科（埃博拉）等不同家族的病毒融合蛋白具有共同的结构特征，并提示了共同的膜融合机制。
The ectodomain of the Ebola virus Gp2 glycoprotein was solubilized with a trimeric, isoleucine zipper derived from GCN4 (pIIGCN4) in place of the hydrophobic fusion peptide at the N terminus. This chimeric molecule forms a trimeric, highly alpha-helical, and very thermostable molecule, as determined by chemical crosslinking and circular dichroism. Electron microscopy indicates that Gp2 folds into a rod-like structure like influenza HA2 and HIV-1 gp41, providing further evidence that viral fusion proteins from diverse families such as Orthomyxoviridae (Influenza), Retroviridae (HIV-1), and Filoviridae (Ebola) share common structural features, and suggesting a common membrane fusion mechanism.