Physical association between the EBV protein EBNA-1 and P32/TAP/hyaluronectin

M R Chen, J F Yang, C W Wu, J M Middeldorp, J Y Chen

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Epstein-Barr virus (EBV) nuclear antigen-1 (EBNA-1) is a protein expressed constitutively during EBV latency. It is required to support the replication of the EBV genome once per cell cycle via the latent origin of replication, oriP. EBNA-1 also can activate transcription through binding to the family repeats of oriP. We wished to identify candidate cellular protein(s) that may interact with EBNA-1 and mediate these functions. A 32-kd protein was co-immunoprecipitated with EBNA-1 from 293 cells using a monoclonal antibody EBNA.OT1x. The regions of EBNA-1 which interact with this protein were studied using two deletion clones and mapped to EBNA-1 residues 1-102 and 325-357. Deletion of this region was shown previously in a mutant of EBNA-1 which had dominant-negative effects on both DNA replication and transactivation assays. The 32-kd protein was found to react with a polyclonal antiserum against P32/TAP (HIV Tat associated protein), which is known to interact with other RNA binding proteins and the RNA splicing factor SF2. The function of P32 was therefore proposed to involve RNA processing. In addition, this molecule was recently identified as hyaluronectin, which binds hyaluronic acid. Because several reports documented that intracellular hyaluronic acid can potentially affect cell proliferation, the association between EBNA-1 and P32/TAP/hyaluronectin may help the maintenance of episomal viral DNA within proliferating cells.

Original languageEnglish
Pages (from-to)173-9
Number of pages7
JournalAnnals of biomedical engineering
Issue number3
Publication statusPublished - 1998


  • Animals
  • Antibodies, Viral
  • Antigens, Viral
  • Binding Sites
  • Blotting, Western
  • Carrier Proteins
  • Cells, Cultured
  • Epstein-Barr Virus Nuclear Antigens
  • Glycoproteins
  • Humans
  • Journal Article
  • Precipitin Tests
  • Rabbits
  • Research Support, Non-U.S. Gov't
  • Transfection

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