Interactions of Marburg virus nucleocapsid proteins
Interactions of Marburg virus nucleocapsid proteins
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DOI：
10.1006/viro.1998.9328
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发表时间：
1998-09-30
期刊：
影响因子：
3.7
通讯作者：
Mühlberger, E
中科院分区：
文献类型：
--
作者：
Becker, S;Rinne, C;Mühlberger, E
本研究测定了马尔堡病毒核衣壳复合物的组分，并研究了化合物之间的相互作用。利用盐解离分离的病毒粒子。四种蛋白质（NP、VP 35、VP 30和L）保持与核心复合物连接。相同的蛋白质被检测到细胞内被定位在MBGV诱导的包涵体，这被认为是代表区域的核衣壳形成。为了研究这四种蛋白之间的相互作用，进行了共表达蛋白的免疫荧光分析。VP 35和VP 30在NP诱导的包涵体中重新分布，证明了NP-VP 35和NP-VP 30之间形成复合物。此外，通过免疫共沉淀法检测到L和VP 35之间的复合物。利用L的缺失突变体，可以将L上的VP 35的结合位点限制在N端530个氨基酸残基。NP、VP 35和L的共表达导致VP 35连接NP和L形成三重复合物。推测检测到的复合物代表MBGV转录和复制机制的关键组分（C）1998 Academic Press。
In this study, the components of Marburg virus nucleocapsid complex were determined, and interactions between the compounds were investigated. Using salt dissociation of isolated virions. four proteins (NP, VP35, VP30, and L) remained attached to the core complex. Same proteins were detected intracellularly to be localized in MBGV-induced inclusion bodies, which are presumed to represent areas of nucleocapsid formation. To investigate interactions between the four proteins, immunofluorescence analysis of coexpressed proteins was carried out. Complexes between NP-VP35 and NP-VP30 were formed, which was demonstrated by redistribution of VP35 and VP30 into NP-induced inclusion bodies. Furthermore, complexes between L and VP35 were detected by coimmunoprecipitation. Using deletion mutants of L, the binding site of VP35 on L could be restricted to the N-terminal 530 amino-acid residues. Coexpression of NP, VP35, and L led to the formation of a triple complex where VP35 linked NP and L. The detected complexes are presumed to represent the key components of the MBGV transcription and replication machinery (C) 1998 Academic Press.