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

National Laboratory for Zoonotic Diseases and Special Pathogens, National Microbiology Laboratory, Public Health Agency of Canada, 1015 Arlington Street, Winnipeg R3E 3R2, Canada.
Virus Research (Impact Factor: 2.83). 12/2008; 140(1-2):8-14. DOI: 10.1016/j.virusres.2008.10.017
Source: PubMed

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.

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Available from: Thomas Hoenen, Jul 27, 2015
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    • "In addition to NP, the RNP complex also contains the viral RNA genome, the polymerase (L), the polymerase cofactor (VP35) and the transcriptional activator (VP30). NP has been shown to directly interact with VP35 and VP30, both of which interact with L (Becker et al., 1998; Groseth et al., 2009). "
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