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The latent membrane protein‐1 in Epstein‐Barr virus‐transformed lymphoblastoid cells is found with ubiquitin‐protein conjugates and heat‐shock protein 70 in lysosomes oriented around the microtubule organizing centre
Author(s) -
Lázló Lajos,
Tuckwell Jayne,
Self Tim,
Lowe James,
Landon Michael,
Smith Sharon,
Hawthorne John N.,
Mayer R. John
Publication year - 1991
Publication title -
the journal of pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.964
H-Index - 184
eISSN - 1096-9896
pISSN - 0022-3417
DOI - 10.1002/path.1711640305
Subject(s) - immunogold labelling , microtubule , microbiology and biotechnology , biology , microtubule organizing center , intermediate filament , heat shock protein , vimentin , epstein–barr virus , chemistry , virus , virology , cytoskeleton , biochemistry , cell , antibody , immunology , centrosome , immunohistochemistry , cell cycle , gene
Immunofluorescence studies on Epstein‐Barr virus (EBV)‐transformed lymphoblastoid cells have previously shown that the latent membrane transforming protein (LMP‐1) is found in patch‐like inclusions which also immunostain for vimentin. We now show that EBV transformation causes a major reorganization of intermediate filaments, microtubules, mitochondria, and lysosomal elements, which generally become oriented around the microtubute organizing centre. Immunogold electron microscopy shows that LMP‐1 is primarily concentrated in secondary lysosomes together with ubiquitin‐protein conjugates and heat‐shock protein 70. Intermediate filament inclusion formation with the above characteristics may be a general response triggered by other membrane glycoproteins; as seen, for example, in major human neurodegenerative diseases such as diffuse Lewy body disease.