Epstein–Barr virus BDLF2–BMRF2 complex affects cellular morphology

• DOI: 10.1099/vir.0.009571-0
• Publication Date: 2009-05-18T18:28:53Z
• Authors: Jens-Bernhard Loe...; Stefano Di Fiore; Klaus Ritter; Rainer Fischer; Michael Kleines
• Keywords: Mammals; 0301 basic medicine; Herpesvirus 4, Human; 0303 health sciences; Membrane Glycoproteins; Cell Membrane; Golgi Apparatus; Endoplasmic Reticulum; Cell Line; 3. Good health; Viral Proteins; 03 medical and health sciences; Viral Envelope Proteins; Animals; Humans; rhoA GTP-Binding Protein; Cell Shape; Cytoskeleton; Protein Binding

Herpesvirus glycoproteins often form specific heterodimers that can fulfil functions cannot be carried out by either of the partners acting alone. This study showed interactions between Epstein–Barr virus (EBV) multi-spanning transmembrane envelope protein BMRF2 and type II membrane BDLF2 influence way in which these proteins are trafficked cell, hence subcellular compartment they accumulate. When expressed transiently mammalian cells, accumulated endoplasmic reticulum (ER), whereas ER Golgi apparatus. However, when two were co-expressed, was transported with to apparatus from there plasma membrane, where co-localized extensively. The distribution at reproducibly associated dramatic changes cellular morphology, including formation enlarged protrusions processes whose adhesion extremities organized actin cytoskeleton. A dominant-active small GTPase RhoA epistatic this morphological phenotype, suggesting is a central component signalling pathway reorganizes cytoskeleton response BDLF2–BMRF2. It concluded EBV produces glycoprotein heterodimer induces morphology through reorganization may facilitate virion spread cells.