A truncated T antigen expressed from an alternatively spliced BK virus early mRNA.

The early region of BK virus (BKV) is known to encode two well-characterized tumour (T) antigens, large T antigen (TAg) and small T antigen (tAg). In this study, we provide evidence of a third early BKV mRNA that codes for an additional early region product with an apparent molecular mass of 17-20 kDa. This truncated form of TAg (truncTAg) is expressed from an alternatively spliced mRNA that is derived from the excision of a second intron from the mRNA encoding TAg.

BK virus as a cofactor in the etiology of prostate cancer in its early stages.

Prostate cancer has been projected to cause almost 10% of all male cancer deaths in the United States in 2007. The incidence of mutations in the tumor suppressor genes Rb1 and p53, especially in the early stages of the disease, is low compared to those for other cancers. This has led to the hypothesis that a human virus such as BK virus (BKV), which establishes a persistent subclinical infection in the urinary tract and encodes oncoproteins that interfere with these tumor suppressor pathways, is involved.

Detection and expression of human BK virus sequences in neoplastic prostate tissues.

BK virus (BKV) is ubiquitous in the human population and establishes a lifelong, subclinical persistent infection in the urinary tract. When the immune system is compromised, it can cause severe disease in the kidney and bladder. Detection of BKV sequences in urinary tract neoplasms has led to the postulate that this virus may induce human oncogenesis through the function of its large tumor antigen (TAg).

High mobility group B proteins facilitate strong estrogen receptor binding to classical and half-site estrogen response elements and relax binding selectivity.

The estrogen receptor alpha (ER) is a ligand-dependent transcription factor that regulates the expression of estrogen-responsive genes. A key step in the activation process is the initial binding of the ER dimer to the estrogen response element (ERE). We examined the effect of the coactivator proteins, HMGB1 and HMGB2, in enhancing ER binding affinity to single and tandem EREs.