EBV BMRF-2 facilitates cell-to-cell spread of virus within polarized oral epithelial cells

• Published in: Virology (New York, N.Y.) Vol. 388; no. 2; pp. 335 - 343
• Main Authors: Xiao, Jianqiao, Palefsky, Joel M, Herrera, Rossana, Berline, Jennifer, Tugizov, Sharof M
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 05.06.2009
• Subjects: Cell Line, Tumor; EBV BMRF-2; EBV cell-to-cell spread; Epithelial Cells - cytology; Epithelial Cells - metabolism; Epithelial Cells - virology; Epstein-Barr virus; Herpesvirus 4, Human - chemistry; Herpesvirus 4, Human - genetics; Herpesvirus 4, Human - physiology; Humans; Infectious Disease; Lymphocytes - metabolism; Lymphocytes - virology; Membrane Glycoproteins - genetics; Membrane Glycoproteins - metabolism; Mouth - cytology; Mouth - virology; Protein Sorting Signals; Protein Transport; Viral Proteins - genetics; Viral Proteins - metabolism; EBV BMRF-2; EBV cell-to-cell spread
• ISSN: 0042-6822; 1096-0341
• DOI: 10.1016/j.virol.2009.03.030

Abstract We previously reported that the Epstein–Barr virus (EBV) BMRF-2 protein plays an important role in EBV infection of polarized oral epithelial cells by interacting with β1 and αv family integrins. Here we show that infection of polarized oral epithelial cells with B27-BMRF-2low recombinant virus, expressing a low level of BMRF-2, resulted in significantly smaller plaques compared with infection by parental B95-8 virus. BMRF-2 localized in the trans-Golgi network (TGN) and basolateral sorting vesicles and was transported to the basolateral membranes of polarized epithelial cells. Mutation of the tyrosine- and dileucine-containing basolateral sorting signal, YLLV, in the cytoplasmic domain of BMRF-2 led to the failure of its accumulation in the TGN and its basolateral transport. These data show that BMRF-2 may play an important role in promoting the spread of EBV progeny virions through lateral membranes of oral epithelial cells.