PDF(Pubmed)
Abstract：
We report the first cryoEM structure of the Hendra henipavirus nucleoprotein in complex with RNA, at 3.5 Å resolution, derived from single particle analysis of a double homotetradecameric RNA-bound N protein ring assembly exhibiting D14 symmetry. The structure of the HeV N protein adopts the common bi-lobed paramyxoviral N protein fold; the N-terminal and C-terminal globular domains are bisected by an RNA binding cleft containing six RNA nucleotides and are flanked by the N-terminal and C-terminal arms, respectively. In common with other paramyxoviral nucleocapsids, the lateral interface between adjacent Ni and Ni+1 protomers involves electrostatic and hydrophobic interactions mediated primarily through the N-terminal arm and globular domains with minor contribution from the C-terminal arm. However, the HeV N multimeric assembly uniquely identifies an additional protomer-protomer contact between the Ni+1 N-terminus and Ni-1 C-terminal arm linker. The model presented here broadens the understanding of RNA-bound paramyxoviral nucleocapsid architectures and provides a platform for further insight into the molecular biology of HeV, as well as the development of antiviral interventions.
摘要：
我们报道了Hendrahenipavirus核蛋白与RNA复合的第一个冷冻EM结构，在3.5μ分辨率下，来自对表现出D14对称性的双同源十聚体RNA结合的N蛋白环组装的单颗粒分析。HeVN蛋白的结构采用常见的双瓣副粘病毒N蛋白折叠；N端和C端球形结构域被包含六个RNA核苷酸的RNA结合裂口一分为二，侧翼为N端和C端臂，分别。与其他副粘病毒核衣壳一样，相邻Ni和Ni1质子之间的横向界面涉及主要通过N端臂和球状结构域介导的静电和疏水相互作用，而C端臂的贡献较小。然而,HeVN多聚体组装独特地识别了Ni1N末端和Ni-1C末端臂接头之间的额外的质子-质子接触。这里提出的模型拓宽了对RNA结合的副粘病毒核衣壳结构的理解，并为进一步了解HeV的分子生物学提供了平台。以及抗病毒干预措施的发展。
