Human importin alpha and RNA do not compete for binding to influenza A virus nucleoprotein
Human importin alpha and RNA do not compete for binding to influenza A virus nucleoprotein
复制标题
DOI：
10.1016/j.virol.2010.10.001
复制
发表时间：
2011-01-05
期刊：
影响因子：
3.7
通讯作者：
Baudin, Florence
中科院分区：
文献类型：
--
作者：
Boulo, Sebastien;Akarsu, Hatice;Baudin, Florence
流感病毒有一个由8个负链RNA片段组成的分段基因组。每个片段都覆盖着NP形成核糖核蛋白(VRNPs)，并携带异源三聚体聚合酶复合体的副本。作为RNA病毒中的一种罕见现象，病毒的复制发生在细胞核内，因此意味着宿主与病毒因子之间的相互作用，如Importinα与核蛋白之间的相互作用。在本研究中，我们报道了通过与人核受体Importin Alpha 5(Imp Alpha 5)结合，病毒NP不再是低聚物，而是以单体形式存在于复合体中。在这方面，Imp Alpha 5充当伴侣，直到NP被运送到细胞核中进行病毒RNA的包裹。此外，我们还表明，NP与宿主转运蛋白的结合不会损害NP与RNA的结合。复杂的人Impα5-NP与RNA的亲和力与wt NP的亲和力相同，而工程单体NP通过点突变与RNA的亲和力大大降低。(C)2010 Elsevier Inc.保留所有权利。
Influenza virus has a segmented genome composed of eight negative stranded RNA segments. Each segment is covered with NP forming ribonucleoproteins (vRNPs) and carries a copy of the heterotrimeric polymerase complex. As a rare phenomenon among the RNA viruses, the viral replication occurs in the nucleus and therefore implies interactions between host and viral factors, such as between importin alpha and nucleoprotein. In the present study we report that through binding with the human nuclear receptor importin alpha 5 (Imp alpha 5), the viral NP is no longer oligomeric but maintained as a monomer inside the complex. In this regard, Imp alpha 5 acts as a chaperone until NP is delivered in the nucleus for viral RNA encapsidation. Moreover, we show that the association of NP with the host transporter does not impair the binding of NP to RNA. The complex human Imp alpha 5-NP binds RNA with the same affinity as wt NP alone, whereas engineered monomeric NP through point mutations binds RNA with a strongly reduced affinity. (C) 2010 Elsevier Inc. All rights reserved.