Elsevier

Virology

Volume 370, Issue 2, 20 January 2008, Pages 430-442
Virology

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

https://doi.org/10.1016/j.virol.2007.09.012Get rights and content
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Abstract

We previously reported that BMRF-2, an Epstein–Barr virus (EBV) glycoprotein, binds to β1 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.

Keywords

Epstein–Barr virus
BMRF-2
Integrin
Virion attachment
Oral epithelial cells

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