埃博拉病毒核糖核蛋白复合体：一种新发现的VP30-L相互作用
The Ebola virus ribonucleoprotein complex: a novel VP30-L interaction identified.
作者信息
Groseth A, Charton J E, Sauerborn M, Feldmann F, Jones S M, Hoenen T, Feldmann H
机构信息
National Laboratory for Zoonotic Diseases and Special Pathogens, National Microbiology Laboratory, Public Health Agency of Canada, 1015 Arlington Street, Winnipeg R3E 3R2, Canada.
出版信息
Virus Res. 2009 Mar;140(1-2):8-14. doi: 10.1016/j.virusres.2008.10.017. Epub 2008 Dec 16.
The ribonucleoprotein (RNP) complex of Ebola virus (EBOV) is known to be a multiprotein/RNA structure, however, knowledge is rather limited regarding the actual protein-protein interactions involved in its formation. Here we show that singularly expressed VP35 and VP30 are present throughout the cytoplasm, while NP forms prominent cytoplasmic inclusions and L forms smaller perinuclear inclusions. We could demonstrate the existence of NP-VP35, NP-VP30 and VP35-L interactions, similar to those described for Marburg virus (MARV) based on the redistribution of protein partners into NP and L inclusion bodies. Significantly, a novel VP30-L interaction was also identified and found to form as part of an NP-VP30-L bridge structure, similar to that formed by VP35. The identification of these interactions allows a preliminary model of the EBOV RNP complex structure to be proposed, and may provide insight into filovirus transcriptional regulation.
已知埃博拉病毒（EBOV）的核糖核蛋白（RNP）复合体是一种多蛋白/RNA结构，然而，对于其形成过程中实际涉及的蛋白质-蛋白质相互作用，人们了解得相当有限。在此我们表明，单独表达的VP35和VP30遍布整个细胞质，而核蛋白（NP）形成明显的细胞质内含物，而L蛋白形成较小的核周内含物。基于蛋白质伙伴重新分布到NP和L内含体中，我们能够证明NP-VP35、NP-VP30和VP35-L相互作用的存在，这与马尔堡病毒（MARV）所描述的相互作用类似。值得注意的是，还鉴定出一种新型的VP30-L相互作用，并发现其作为NP-VP30-L桥结构的一部分形成，类似于由VP35形成的结构。这些相互作用的鉴定使得能够提出EBOV RNP复合体结构的初步模型，并可能为丝状病毒转录调控提供见解。
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