title: The Epstein-Barr virus BMRF-2 protein facilitates virus attachment to oral epithelial cells.
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.
authors.affiliation: Department of Medicine, University of California, San Francisco, CA 94143-0654, USA.
authors.forename: Jianqiao
authors.initials: J
authors.lastname: Xiao
authors.forename: Joel M
authors.initials: JM
authors.lastname: Palefsky
authors.forename: Rossana
authors.initials: R
authors.lastname: Herrera
authors.forename: Jennifer
authors.initials: J
authors.lastname: Berline
authors.forename: Sharof M
authors.initials: SM
authors.lastname: Tugizov
mesh_terms: D019943:Amino Acid Substitution; D000818:Animals; D001402:B-Lymphocytes / Q000821:virology; D001483:Base Sequence; D002144:Callithrix; D002460:Cell Line; D016764:Cell Polarity; D017931:DNA Primers / Q000235:genetics; D004279:DNA, Viral / Q000235:genetics; D004847:Epithelial Cells / Q000821:virology; D004854:Herpesvirus 4, Human / Q000235:genetics / Q000472:pathogenicity* / Q000502:physiology*; D006801:Humans; D019012:Integrin beta1 / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D009055:Mouth / Q000166:cytology / Q000821:virology; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D009842:Oligopeptides; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011995:Recombination, Genetic; D014764:Viral Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D019065:Virus Assembly
chemical_list: C109482:BMRF-2 protein, Human herpesvirus 4; D017931:DNA Primers; D004279:DNA, Viral; D019012:Integrin beta1; D008562:Membrane Glycoproteins; D009842:Oligopeptides; D011994:Recombinant Proteins; D014764:Viral Proteins; C047981:arginyl-glycyl-aspartic acid