Institut de Biologie Structurale (IBS), Univ. Grenoble Alpes, CEA, CNRS, 38044, Grenoble, France.
IHAP, Université de Toulouse, INRA, ENVT, Toulouse, France.
Sci Rep. 2019 Jan 24;9(1):600. doi: 10.1038/s41598-018-37306-y.
This paper focuses on the nucleoprotein (NP) of the newly identified member of the Orthomyxoviridae family, Influenza D virus. To date several X-ray structures of NP of Influenza A (A/NP) and B (B/NP) viruses and of infectious salmon anemia (ISA/NP) virus have been solved. Here we purified, characterized and solved the X-ray structure of the tetrameric D/NP at 2.4 Å resolution. The crystal structure of its core is similar to NP of other Influenza viruses. However, unlike A/NP and B/NP which possess a flexible amino-terminal tail containing nuclear localization signals (NLS) for their nuclear import, D/NP possesses a carboxy-terminal tail (D/NP). We show that D/NP harbors a bipartite NLS and designed C-terminal truncated mutants to demonstrate the role of D/NP for nuclear transport.
本文主要关注 Orthomyxoviridae 科新鉴定成员的核蛋白(NP),即流感 D 病毒。迄今为止,已经解析了几种 A 型(A/NP)和 B 型(B/NP)流感病毒以及传染性鲑鱼贫血(ISA/NP)病毒的 NP 的 X 射线结构。在这里,我们纯化、鉴定并解析了四聚体 D/NP 的 X 射线结构,分辨率为 2.4Å。其核心的晶体结构与其他流感病毒的 NP 相似。然而,与具有核定位信号(NLS)的灵活氨基末端尾巴,用于核输入的 A/NP 和 B/NP 不同,D/NP 具有羧基末端尾巴(D/NP)。我们表明,D/NP 具有二分位 NLS,并设计了 C 末端截断突变体以证明 D/NP 对核转运的作用。