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. 2008 Dec 5;377(1):93-7.
doi: 10.1016/j.bbrc.2008.09.082. Epub 2008 Sep 26.

Viral hijacking of human receptors through heterodimerization

Henry F Vischer  1 , Saskia Nijmeijer, Martine J Smit, Rob Leurs
Affiliations

Viral hijacking of human receptors through heterodimerization

Henry F Vischer et al. Biochem Biophys Res Commun. .

Abstract

Epstein-Barr virus (EBV) is a human herpesvirus that primarily infects B lymphocytes and is associated with tumor development. Like other herpesviruses, EBV has pirated and modified host genes encoding important regulatory cellular proteins to take over cellular control after infection. One of these genes (BILF1) encodes a G protein-coupled receptor (GPCR). It is currently accepted that GPCRs exist and function as dimers. B lymphocyte migration and functioning is regulated by chemokines acting on their cognate receptors. In this study, we show that BILF1 heterodimerizes with various chemokine receptors using BRET, trFRET and co-immunoprecipitation. Importantly, heterodimerization of BILF1 with chemokine receptors may alter the responsiveness of B lymphocytes to chemokines thereby altering homing and homeostasis of infected B lymphocytes and might be essential for EBV dissemination and/or involved in EBV-induced pathogenesis.

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