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Journal of Virology, March 2008, p. 2230-2240, Vol. 82, No. 5
0022-538X/08/$08.00+0     doi:10.1128/JVI.02285-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

SIAH-1 Interacts with the Kaposi's Sarcoma-Associated Herpesvirus-Encoded ORF45 Protein and Promotes Its Ubiquitylation and Proteasomal Degradation{triangledown}

Rinat Abada, Tsofia Dreyfuss-Grossman, Yifat Herman-Bachinsky, Haim Geva, Shiri-Rivka Masa, and Ronit Sarid*

The Mina and Everard Goodman Faculty of Life Sciences, Bar Ilan University, Ramat-Gan, Israel

Received 22 October 2007/ Accepted 3 December 2007

Kaposi's sarcoma-associated herpesvirus (KSHV), also referred to as human herpesvirus 8, is a potentially tumorigenic virus implicated in the etiology of Kaposi's sarcoma, primary effusion lymphoma, and some forms of multicentric Castleman's disease. The open reading frame 45 (ORF45) protein, encoded by the KSHV genome, is capable of inhibiting virus-dependent interferon induction and appears to be essential for both early and late stages of infection. In the present study, we show, both in yeast two-hybrid assays and in mammalian cells, that the ORF45 protein interacts with the cellular ubiquitin E3 ligase family designated seven in absentia homologue (SIAH). We provide evidence that SIAH-1 promotes the degradation of KSHV ORF45 through a RING domain-dependent mechanism and via the ubiquitin-proteasome system. Furthermore, our data indicate the involvement of SIAH-1 in the regulation of the expression of ORF45 in KSHV-infected cells. Since the availability of KSHV ORF45 is expected to influence the course of KSHV infection, our findings identify a novel biological role for SIAH proteins as modulators of virus infection.

* Corresponding author. Mailing address: The Mina and Everard Goodman Faculty of Life Sciences, Bar Ilan University, Ramat-Gan, Israel 52900. Phone: 972-3-5317853. Fax: 972-3-7384058. E-mail: saridr{at}mail.biu.ac.il

{triangledown} Published ahead of print on 12 December 2007.

Journal of Virology, March 2008, p. 2230-2240, Vol. 82, No. 5
0022-538X/08/$08.00+0     doi:10.1128/JVI.02285-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Kuang, E., Wu, F., Zhu, F. (2009). Mechanism of Sustained Activation of Ribosomal S6 Kinase (RSK) and ERK by Kaposi Sarcoma-associated Herpesvirus ORF45: MULTIPROTEIN COMPLEXES RETAIN ACTIVE PHOSPHORYLATED ERK AND RSK AND PROTECT THEM FROM DEPHOSPHORYLATION. J. Biol. Chem. 284: 13958-13968 [Abstract] [Full Text]  
  • Li, X., Zhu, F. (2009). Identification of the Nuclear Export and Adjacent Nuclear Localization Signals for ORF45 of Kaposi's Sarcoma-Associated Herpesvirus. J. Virol. 83: 2531-2539 [Abstract] [Full Text]  


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