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- Title
DRBP76 associates with Ebola virus VP35 and suppresses viral polymerase function.
- Authors
Shabman, Reed S; Leung, Daisy W; Johnson, Joshua; Glennon, Nicole; Gulcicek, Erol E; Stone, Kathryn L; Leung, Lawrence; Hensley, Lisa; Amarasinghe, Gaya K; Basler, Christopher F
- Abstract
The Zaire Ebola virus (EBOV) protein VP35 is multifunctional; it inhibits IFN-α/β production and functions as a cofactor of the viral RNA polymerase. Mass spectrometry identified the double stranded RNA binding protein 76 (DRBP76/NFAR-1/NF90) as a cellular factor that associates with the VP35 C-terminal interferon inhibitory domain (IID). DRBP76 is described to regulate host cell protein synthesis and play an important role in host defense. The VP35-IID-DRBP76 interaction required the addition of exogenous dsRNA, but full-length VP35 associated with DRBP76 in the absence of exogenous dsRNA. Cells infected with a Newcastle disease virus (NDV)-expressing VP35 redistributed DRBP76 from the nucleus to the cytoplasm, the compartment in which EBOV replicates. Overexpression of DRBP76 did not alter the ability of VP35 to inhibit type I IFN production but did impair the function of the EBOV transcription/replication complex. These data suggest that DRBP76, via its association with VP35, exerts an anti-EBOV function.
- Publication
Journal of Infectious Diseases, 2011, Vol 204, Issue 9, pS911
- ISSN
0022-1899
- Publication type
journal article
- DOI
10.1093/infdis/jir343