gH/gL supercomplexes at early stages of herpesvirus entry.
gH/gL supercomplexes at early stages of herpesvirus entry.
复制标题
DOI：
10.1016/j.coviro.2016.01.010
复制
发表时间：
2016-06
影响因子：
5.9
通讯作者：
Heldwein EE
中科院分区：
文献类型：
--
作者：
Heldwein EE
疱疹病毒进入宿主细胞过程中的膜融合是一个复杂的过程，其中多个糖蛋白相互作用，通过保守的异源二聚体Gh/gl将触发信号从受体结合蛋白传递到保守的FusoGen GB。单个糖蛋白的晶体结构是可用的，但高阶“超复合体”一直难以捉摸。人类巨细胞病毒或Epstein-Barr病毒的Gh/gl与疱疹病毒进入早期形成的受体结合蛋白之间的复合物的最新结构突出了控制趋向性的机制，并揭示了含有Gh/gl的动态中间复合体，可能直接参与了膜的变形和并列。确定触发信号如何到达FusoGen GB代表了疱疹病毒进入的结构生物学的下一个前沿。
Membrane fusion during herpesvirus entry into host cells is a complex process where multiple glycoproteins interact to relay the triggering signal from a receptor-binding protein to the conserved fusogen gB through the conserved heterodimer gH/gL. Crystal structures of individual glycoproteins are available, yet high-order “supercomplexes” have been elusive. Recent structures of complexes between gH/gL from human cytomegalovirus or Epstein-Barr virus and the receptor-binding proteins that form at early stages of herpesviral entry highlighted mechanisms that control tropism and revealed dynamic intermediate complexes containing gH/gL that may directly participate in membrane deformation and juxtaposition. Determining how the triggering signal reaches the fusogen gB represents the next frontier in structural biology of herpesvirus entry.