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Journal of Virology, May 2008, p. 4275-4283, Vol. 82, No. 9
0022-538X/08/$08.00+0 doi:10.1128/JVI.02249-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Wentao Qiao,
Jian Wang,
Fengwen Xu,
Yue Li,
Jun Zhou,
Qimin Chen, and
Yunqi Geng*
Key Laboratory of Molecular Microbiology and Biotechnology (Ministry of Education) and Key Laboratory of Microbial Functional Genomics (Tianjin), College of Life Sciences, Nankai University, Tianjin 300071, China
Received 17 October 2007/ Accepted 16 February 2008
Interferon-induced proteins (IFPs) exert multiple functions corresponding to diverse interferon signals. However, the intracellular functions of many IFPs are not fully characterized. Here, we report that IFP35, a member of the IFP family with a molecular mass of 35 kDa, can interact with the bovine Tas (BTas) regulatory protein of bovine foamy virus (BFV). The interaction involves NID2 (IFP35/Nmi homology domain) of IFP35 and the central domain of BTas. The overexpression of IFP35 disturbs the ability of BTas to activate viral-gene transcription and inhibits viral replication. The depletion of endogenous IFP35 by interfering RNA can promote the activation of BFV, suggesting an inhibitory function of IFP35 in viral-gene expression. In addition, IFP35 can interact with the homologous regulatory protein of prototype FV and arrest viral replication and repress viral transcription. Our study suggests that IFP35 may represent a novel pathway of interferon-mediated antiviral activity in host organisms that plays a role in the maintenance of FV latency.
Published ahead of print on 27 February 2008.
J.T. and W.Q. contributed equally to this work.
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