Identification of Epstein-Barr virus RK-BARF0-interacting proteins and characterization of expression pattern

J Virol. 2004 Dec;78(23):12848-56. doi: 10.1128/JVI.78.23.12848-12856.2004.

Abstract

The Epstein-Barr virus (EBV) BamHI A transcripts are a family of transcripts that are differentially spliced and can be detected in multiple EBV-associated malignancies. Several of the transcripts may encode proteins. One transcript of interest, RK-BARF0, is proposed to encode a 279-amino-acid protein with a possible endoplasmic reticulum-targeting sequence. In this study, the properties of RK-BARF0 were examined through identification of cellular-interacting proteins through yeast two-hybrid analysis and characterization of its expression in EBV-infected cells and tumors. In addition to the interaction previously identified with cellular Notch, it was determined that RK-BARF0 also bound cellular human I-mfa domain-containing protein (HIC), epithelin, and scramblase. An interaction between RK-BARF0 and Notch or epithelin induced proteasome-dependent degradation of Notch and epithelin but not of HIC or scramblase. Low levels of endogenous Notch expression in EBV-positive cell lines may correlate with RK-BARF0 expression. However, a screen of EBV-positive cell lines and tumors with an affinity-purified alpha-RK-BARF0 antiserum did not consistently detect RK-BARF0. These data suggest that while RK-BARF0 may have important cellular functions during EBV infection, and while the phenotype of EBV-positive cells suggest its expression, RK-BARF0 levels may be too low to detect.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Granulins
  • Intercellular Signaling Peptides and Proteins / metabolism
  • Membrane Proteins / metabolism
  • Molecular Sequence Data
  • Proteasome Endopeptidase Complex / physiology
  • Protein Binding
  • Rabbits
  • Receptors, Notch
  • Viral Proteins / analysis
  • Viral Proteins / chemistry
  • Viral Proteins / metabolism*

Substances

  • Granulins
  • Intercellular Signaling Peptides and Proteins
  • Membrane Proteins
  • RK-BARF0 protein, Human herpesvirus 4
  • Receptors, Notch
  • Viral Proteins
  • Proteasome Endopeptidase Complex