@article{mbs:/content/journal/jgv/10.1099/vir.0.18944-0, author = "Flanagan, James and Middeldorp, Jaap and Sculley, Tom", title = "Localization of the Epstein–Barr virus protein LMP 1 to exosomes", journal= "Journal of General Virology", year = "2003", volume = "84", number = "7", pages = "1871-1879", doi = "https://doi.org/10.1099/vir.0.18944-0", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.18944-0", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "The Epstein–Barr virus latent membrane protein (LMP 1) functions as a constitutively active signalling molecule and associates in lipid rafts clustered with other signalling molecules. Using immunofluorescent confocal microscopy, LMP 1 was shown to have an heterogeneous distribution among individual cells which was not related to the cell cycle stage. LMP 1 was shown to localize to intracellular compartments in cells other than the plasma membrane. Co-labelling of cells with both an LMP 1 antibody and an antibody to the Golgi protein GS15 revealed that the intracellular LMP 1 partly co-localized with the Golgi apparatus. Further confirmation of intracellular LMP 1 localization was obtained by immunoelectron microscopy with rabbit polyclonal LMP 1 antibodies and cryosectioning. As well as being present in intracellular foci, LMP 1 co-localized in part with MHC-II and was present on exosomes derived from a lymphoblastoid cell line. Preparations of LMP 1 containing exosomes were shown to inhibit the proliferation of peripheral blood mononuclear cells, suggesting that LMP 1 could be involved in immune regulation. This may be of particular relevance in EBV-associated tumours such as nasopharyngeal carcinoma and Hodgkin's disease, as LMP 1-containing exosomes may be taken up by infiltrating T-lymphocytes, where LMP 1 could exert an anti-proliferative effect, allowing the tumour cells to evade the immune system.", }