The Epstein-Barr virus BMRF-2 protein facilitates virus attachment to oral epithelial cells

Virology. 2008 Jan 20;370(2):430-42. doi: 10.1016/j.virol.2007.09.012. Epub 2007 Oct 22.

Abstract

We previously reported that BMRF-2, an Epstein-Barr virus (EBV) glycoprotein, binds to beta1 family integrins and is important for EBV infection of polarized oral epithelial cells. To further study the functions of BMRF-2, we constructed a recombinant EBV that lacks BMRF-2 expression by homologous recombination in B95-8 cells. We found that lack of BMRF-2 resulted in about 50% reduction of EBV attachment to oral epithelial cells, but not to B lymphocytes, suggesting that BMRF-2 is critical for EBV infection in oral epithelial cells, but not in B lymphocytes. In polarized oral epithelial cells, infection rate of the recombinant EBV virus was about 4- to 8-fold lower than the wild-type B95-8 virus. Cell adhesion assays using the BMRF-2 RGD peptide and its RGE and AAA mutants showed that the RGD motif is critical for BMRF-2 binding to integrins. These data are consistent with our previous observation that interactions between EBV BMRF-2 and integrins are critical for infection of oral epithelial cells with EBV.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Substitution
  • Animals
  • B-Lymphocytes / virology
  • Base Sequence
  • Callithrix
  • Cell Line
  • Cell Polarity
  • DNA Primers / genetics
  • DNA, Viral / genetics
  • Epithelial Cells / virology
  • Herpesvirus 4, Human / genetics
  • Herpesvirus 4, Human / pathogenicity*
  • Herpesvirus 4, Human / physiology*
  • Humans
  • Integrin beta1 / metabolism
  • Membrane Glycoproteins / chemistry
  • Membrane Glycoproteins / genetics
  • Membrane Glycoproteins / physiology*
  • Mouth / cytology
  • Mouth / virology
  • Mutagenesis, Site-Directed
  • Mutation
  • Oligopeptides
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Recombination, Genetic
  • Viral Proteins / chemistry
  • Viral Proteins / genetics
  • Viral Proteins / physiology*
  • Virus Assembly

Substances

  • BMRF-2 protein, Human herpesvirus 4
  • DNA Primers
  • DNA, Viral
  • Integrin beta1
  • Membrane Glycoproteins
  • Oligopeptides
  • Recombinant Proteins
  • Viral Proteins
  • arginyl-glycyl-aspartic acid