Hepatitis B virus X protein (HBx protein) is a multifunctional regulatory protein. The transactivation of nuclear factor kappa B (NF-κB) by HBx protein has been shown to be of importance in the pathogenesis of HBV-related diseases. However, the mechanism involved remains largely unclear. In this study, a CytoTrap yeast two-hybrid system was employed to screen binding partners of the HBx protein; 29 cellular proteins, including valosin-containing protein (VCP), were identified. The interaction between HBx protein and VCP was further confirmed in vitro and in vivo using a glutathione S-transferase pull-down assay and co-immunoprecipitation, respectively. It was also shown that this interaction is mediated by amino acid residues 51–120 of the HBx protein. In Huh-7 hepatoma cells, HBx protein enhanced the VCP-mediated activation of NF-κB. Our findings provide new insights into the molecular mechanisms that lead to the activation of NF-κB by HBx protein.
Archives of Virology – Springer Journals
Published: Nov 1, 2011
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