Xu Yanhui, Gao Shan, Cole David K, Zhu Junjie, Su Nan, Wang Hui, Gao George F, Rao Zihe
Laboratory of Structural Biology, Tsinghua University, Beijing 100084, China.
Biochem Biophys Res Commun. 2004 Mar 12;315(3):664-70. doi: 10.1016/j.bbrc.2004.01.115.
Nipah virus (NiV) and Hendra virus (HeV) are novel zoonotic members of the Paramyxoviridae family and are the prototypes for a newly designated genus, Genus Henipavirus. Recent studies have shown that paramyxovirus might adopt a similar mechanism of virus fusion-entry. Under this mechanism, the two highly conserved heptad repeat (HR) regions, HR1 and HR2, in the fusion (F) protein, seem to show characteristic structure in the fusion core: the formation of a 6-helix coiled-coil bundle. The three HR1s form the alpha-helix coiled-coil surrounded by three HR2s. In this study, the two HR regions of NiV or HeV were expressed in an Escherichia coli system as a single chain and the results do show that HR1 and HR2 interact with each other in both NiV and HeV and form typical 6-helix coiled-coil bundles. This provides the molecular basis of HR2 inhibition to NiV and HeV fusion as observed in an earlier report.
尼帕病毒（NiV）和亨德拉病毒（HeV）是副粘病毒科新出现的人畜共患病原体，也是新指定的亨尼帕病毒属的原型。最近的研究表明，副粘病毒可能采用类似的病毒融合进入机制。在这种机制下，融合（F）蛋白中两个高度保守的七肽重复（HR）区域，即HR1和HR2，在融合核心似乎呈现出特征性结构：形成一个六螺旋卷曲螺旋束。三个HR1形成被三个HR2包围的α螺旋卷曲螺旋。在本研究中，NiV或HeV的两个HR区域在大肠杆菌系统中作为单链表达，结果确实表明HR1和HR2在NiV和HeV中相互作用，并形成典型的六螺旋卷曲螺旋束。这为早期报告中观察到的HR2抑制NiV和HeV融合提供了分子基础。
