Kuhn Richard J, Zhang Wei, Rossmann Michael G, Pletnev Sergei V, Corver Jeroen, Lenches Edith, Jones Christopher T, Mukhopadhyay Suchetana, Chipman Paul R, Strauss Ellen G, Baker Timothy S, Strauss James H
Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.
Cell. 2002 Mar 8;108(5):717-25. doi: 10.1016/s0092-8674(02)00660-8.
The first structure of a flavivirus has been determined by using a combination of cryoelectron microscopy and fitting of the known structure of glycoprotein E into the electron density map. The virus core, within a lipid bilayer, has a less-ordered structure than the external, icosahedral scaffold of 90 glycoprotein E dimers. The three E monomers per icosahedral asymmetric unit do not have quasiequivalent symmetric environments. Difference maps indicate the location of the small membrane protein M relative to the overlaying scaffold of E dimers. The structure suggests that flaviviruses, and by analogy also alphaviruses, employ a fusion mechanism in which the distal beta barrels of domain II of the glycoprotein E are inserted into the cellular membrane.
黄病毒的首个结构是通过结合冷冻电子显微镜技术以及将糖蛋白E的已知结构拟合到电子密度图中确定的。位于脂质双分子层内的病毒核心，其结构的有序程度低于外部由90个糖蛋白E二聚体组成的二十面体支架。每个二十面体不对称单元中的三个E单体没有准等效的对称环境。差异图显示了小膜蛋白M相对于E二聚体覆盖支架的位置。该结构表明，黄病毒以及类似的甲病毒采用了一种融合机制，即糖蛋白E结构域II的远端β桶插入细胞膜。
