Bovine ephemeral fever rhabdovirus β1 protein has viroporin-like properties and binds importin β1 and importin 7

Joubert, D. Albert, Blasdell, Kim R., Audsley, Michelle D., Trinidad, Lee, Monaghan, Paul, Dave, Keyur A., Lieu, Kim G., Amos-Ritchie, Rachel, Jans, David A., Moseley, Gregory W., Gorman, Jeffrey J. and Walker, Peter J. (2014) Bovine ephemeral fever rhabdovirus β1 protein has viroporin-like properties and binds importin β1 and importin 7. Journal of Virology, 88 3: 1591-1603. doi:10.1128/JVI.01812-13


Author Joubert, D. Albert
Blasdell, Kim R.
Audsley, Michelle D.
Trinidad, Lee
Monaghan, Paul
Dave, Keyur A.
Lieu, Kim G.
Amos-Ritchie, Rachel
Jans, David A.
Moseley, Gregory W.
Gorman, Jeffrey J.
Walker, Peter J.
Title Bovine ephemeral fever rhabdovirus β1 protein has viroporin-like properties and binds importin β1 and importin 7
Journal name Journal of Virology   Check publisher's open access policy
ISSN 0022-538X
1098-5514
Publication date 2014-01-01
Year available 2013
Sub-type Article (original research)
DOI 10.1128/JVI.01812-13
Open Access Status DOI
Volume 88
Issue 3
Start page 1591
End page 1603
Total pages 13
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Collection year 2014
Language eng
Abstract Bovine ephemeral fever virus (BEFV) is an arthropod-borne rhabdovirus that is classified as the type species of the genus Ephemerovirus. In addition to the five canonical rhabdovirus structural proteins (N, P, M, G, and L), the large and complex BEFV genome contains several open reading frames (ORFs) between the G and L genes (α1, α2/α3, β, and γ) encoding proteins of unknown function. We show that the 10.5-kDa BEFV α1 protein is expressed in infected cells and, consistent with previous predictions based on its structure, has the properties of a viroporin. Expression of a BEFV α1-maltose binding protein (MBP) fusion protein in Escherichia coli was observed to inhibit cell growth and increase membrane permeability to hygromycin B. Increased membrane permeability was also observed in BEFV-infected mammalian cells (but not cells infected with an α1-deficient BEFV strain) and in cells expressing a BEFV α1-green fluorescent protein (GFP) fusion protein, which was shown by confocal microscopy to localize to the Golgi complex. Furthermore, the predicted C-terminal cytoplasmic domain of α1, which contains a strong nuclear localization signal (NLS), was translocated to the nucleus when expressed independently, and in an affinity chromatography assay employing a GFP trap, the full-length α1 was observed to interact specifically with importin β1 and importin 7 but not with importin β3. These data suggest that, in addition to its function as a viroporin, BEFV α1 may modulate components of nuclear trafficking pathways, but the specific role thereof remains unclear.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Non HERDC
School of Chemistry and Molecular Biosciences
 
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