| Literature DB >> 19041915 |
A Groseth1, J E Charton, M Sauerborn, F Feldmann, S M Jones, T Hoenen, H Feldmann.
Abstract
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.Entities:
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Year: 2008 PMID： 19041915 PMCID： PMC3398801 DOI： 10.1016/j.virusres.2008.10.017
Source DB: PubMed Journal: Virus Res ISSN： 0168-1702 Impact factor: 3.303