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STP-C, an oncoprotein of Herpesvirus saimiri augments the activation of NF-kappa B through ubiquitination of TRAF6

: Chung, Y.-H.; Jhun, B.H.; Ryu, S.C.; Kim, H.-S.; Kim, C.M.; Kim, B.S.; Kim, Y.O.; Lee, S.J.

Journal of biochemistry and molecular biology 40 (2007), Nr.3, S.341-348
ISSN: 1225-8687
ISSN: 0219-1024
Fraunhofer IGB ()

Herpesvirus saimiri (HVS), a member of the gamma-herpesvirus family, encodes an oncoprotein called Saimiri Transforming Protein (STP) which is required for lymphoma induction in non-human primates. Previous study has shown that STP-C, an oncoprotein of RVS, activates NF-KB signaling pathway. However, the detailed mechanism of STP-C-mediated NF-KB activation has not been reported yet. We first report that STP-C interacts with TRAF6 protein in vivo and in vitro and further investigation shows that Glu(12) residue of STP-C is critical for binding to TRAF6. Introduction of ubiquitin together with STP-C augments NF-KB activity compared to that of STP-C expression alone. STP-C expression further induces ubiquitination of endogenous TRAF6. In addition, either a deubiquitination enzyme, CYLD or a dominant negative E2-conjugation enzyme reduced NF-KB activity in spite of the presence of STP-C, supporting that the interaction between STP-C and TRAF6 induces ubiquitination of TRAF6. NF-KB activation by STP-C through the ubiquitinated TRAF6 causes the increased production of IL-8, an inflammatory chemokine and the enhanced expression of costimulatory molecule ICAM, which might ultimately contribute cellular transformation by the exposure of HVS-infected cells with inflammatory microenvironment and chronic activation.