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Nucleic Acids Research, Vol 24, Issue 23 4741-4750, Copyright © 1996 by Oxford University Press

ARTICLES

XAP2, a novel hepatitis B virus X-associated protein that inhibits X transactivation

N Kuzhandaivelu, YS Cong, C Inouye, WM Yang and E Seto
Moffitt Cancer Center and Research Institute, Department of Medical Microbiology and Immunology, University of South Florida, Tampa 33612, USA.

The hepatitis B virus X protein is a promiscuous transcriptional transactivator. Transactivation by the X protein is most likely mediated through binding to different cellular factors. Using the yeast two-hybrid method, we have isolated a clone that encodes a novel X- associated cellular protein: XAP2. X and XAP2 interactions also occur in vitro. Antiserum raised against XAP2 recognizes a cytoplasmic protein with an apparent molecular mass of 36 kDa. The interaction between X and XAP2 requires a small region on X containing amino acids 13-26. From Northern blot analyses, XAP2 is ubiquitously expressed in both liver-derived and non-liver-derived cell lines as well as in normal non-liver tissues. In contrast, XAP2 is expressed in very low level in the normal human liver. In transfection assays, overexpression of XAP2 abolishes transactivation by the X protein. Based on these results, we suggest that XAP2 is an important cellular negative regulator of the X protein, and that X-XAP2 interaction may play a role in HBV pathology.
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