Epstein-Barr virus encoded nuclear protein EBNA-3 binds XAP-2, a protein associated with Hepatitis B virus X antigen

Elena Kashuba, Vladimir Kashuba, Katja Pokrovskaja, George Klein, Laszlo Szekely

Research output: Contribution to journalArticlepeer-review

40 Scopus citations

Abstract

EBNA-3 (also called EBNA-3A) is one of the EBV encoded nuclear antigens that are necessary for B-cell transformation. EBNA-3 is known to target RBPs, nuclear proteins that also interacts with EBNA-2, EBNA-4 and EBNA-6. In order to identify additional EBNA-3 targets, an EBV-transformed human lymphocyte cDNA library was screened in the yeast two-hybrid system with N-terminus truncated EBNA-3 that cannot interact with RBP-Jκ. A clone, encoding Xap-2 protein, a cellular partner of Hepatitis B virus X-antigen was isolated. This protein is also known as the p38 subunit of the aryl hydrocarbon receptor complex (ARA9). The specific binding to EBNA-3 was confirmed by showing that the CST-Xap-2 precipitated EBNA-3 from CV1 cells that were infected with recombinant vaccinia virus expressing EBNA-3. Deletion of the C-terminus of Xap-2 eliminated the binding. Fusion with green fluorescent protein showed that Xap-2 is preferentially cytoplasmic but translocates to the nucleus upon expression of EBNA-3.

Original languageEnglish
Pages (from-to)1801-1806
Number of pages6
JournalOncogene
Volume19
Issue number14
DOIs
StatePublished - 30 Mar 2000
Externally publishedYes

Keywords

  • EBNA-3
  • HBV
  • Xap-2

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