Identification of an NF-kappa B binding site in the bovine leukemia virus promoter.

Although the mechanism by which bovine leukemia virus (BLV) induces neoplastic transformation of the host B cells is unknown, it is likely that critical interactions between cellular DNA-binding proteins and the virus are involved. We have used DNase I protection (footprinting) assays to construct a map of protein-DNA interactions on the 5' long terminal repeat of BLV. In addition to the three cyclic AMP response elements previously reported, we have also found an NF-kappa B binding site between -118 and -70 nucleotides upstream of the RNA start site. This site binds several members of the kappa B family of proteins, including p49, p50, and p65, in both footprint and electrophoretic mobility shift assays and functions as an enhancer element when inserted upstream of the chloramphenicol acetyltransferase gene. NF-kappa B may be a critical nuclear binding protein that regulates both viral replication and key cellular genes in BLV-infected B cells.     

Expression of LMP1 in epithelial cells leads to the activation of a select subset of NF-kappa B/Rel family proteins.

This study demonstrates that the Epstein-Barr virus protein LMP1 activates a specific subset of NF-kappa B/Rel proteins in the C33 epithelial cell line. Western immunoblot analysis used to analyze the intracellular distribution and abundance of the proteins present in these complexes demonstrated that levels of the p50 and p52 proteins were significantly elevated in the nuclei of LMP1-expressing cells. The data also suggest that LMP1 facilitates the translocation of p50 to the nucleus and may affect the processing of the p100 and p105 precursor proteins or the stability of p52 and p50.