The Ebola virus ribonucleoprotein complex: A novel VP30-L interaction identified

被引：71

作者：

Groseth, A. ^{[1
,2
]}

Charton, J. E. ^{[1
,3
]}

Sauerborn, M. ^{[1
,4
]}

Feldmann, F. ^{[1
]}

Jones, S. M. ^{[1
,5
]}

Hoenen, T. ^{[1
,4
]}

Feldmann, H. ^{[1
,2
]}

机构：

[1] Publ Hlth Agcy Canada, Natl Microbiol Lab, Natl Lab Zoonot Dis & Special Pathogens, Winnipeg, MB R3E 3R2, Canada

[2] Univ Manitoba, Dept Med Microbiol, Winnipeg, MB R3E 0W3, Canada

[3] Univ Tubingen, Intrefak Inst Biochem, D-72076 Tubingen, Germany

[4] Univ Marburg, Inst Virol, D-35043 Marburg, Germany

[5] Univ Manitoba, Dept Immunol, Winnipeg, MB R3E 0W3, Canada

来源：

VIRUS RESEARCH | 2009年 / 140卷 / 1-2期

基金：

加拿大健康研究院; 加拿大自然科学与工程研究理事会;

关键词：

Ebola virus; Polymerase; VP30; Protein-protein interaction; Ribonucleoprotein complex; MARBURG-VIRUS; NUCLEOCAPSID PROTEINS; RNA-POLYMERASE; TRANSCRIPTION; REPLICATION; NUCLEOPROTEIN; RESCUE; SYSTEM; CDNA;

D O I：

10.1016/j.virusres.2008.10.017

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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. Published by Elsevier B.V.

引用

页码：8 / 14

页数：7

共 23 条

[1] Interactions of Marburg virus nucleocapsid proteins [J].