埃博拉病毒糖蛋白膜融合蛋白亚基的核心结构特征是一个长的三链卷曲螺旋。
The central structural feature of the membrane fusion protein subunit from the Ebola virus glycoprotein is a long triple-stranded coiled coil.
作者信息
Weissenhorn W, Calder L J, Wharton S A, Skehel J J, Wiley D C
机构信息
Laboratory of Molecular Medicine, Howard Hughes Medical Institute, The Children's Hospital, 320 Longwood Avenue Boston, MA 02215, USA.
出版信息
Proc Natl Acad Sci U S A. 1998 May 26;95(11):6032-6. doi: 10.1073/pnas.95.11.6032.
Abstract
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.
摘要
埃博拉病毒糖蛋白Gp2的胞外结构域是通过用源自GCN4的三聚异亮氨酸拉链（pIIGCN4）替代N端的疏水融合肽来进行溶解的。通过化学交联和圆二色性测定，这种嵌合分子形成了三聚体、高度α螺旋且非常耐热的分子。电子显微镜显示，Gp2折叠成类似流感HA2和HIV-1 gp41的棒状结构，这进一步证明了正粘病毒科（流感）、逆转录病毒科（HIV-1）和丝状病毒科（埃博拉）等不同病毒家族的病毒融合蛋白具有共同的结构特征，并暗示存在共同的膜融合机制。
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