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Updated: Jun 30, 2026

Engineering Antiviral Agents via Surface Plasmon Resonance
Published on: June 14, 2022
Viral hijacking of human receptors through heterodimerization
Henry F Vischer1, Saskia Nijmeijer, Martine J Smit
1Division of Medicinal Chemistry, Faculty of Sciences, Leiden/Amsterdam Center for Drug Research, VU University Amsterdam, Amsterdam, The Netherlands. vischer@few.vu.nl
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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