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Evidence of LMP1–TRAF3 interactions in glycosphingolipid‐rich complexes of lymphoblastoid and nasopharyngeal carcinoma cells
Author(s) -
ArdilaOsorio Hector,
Clausse Bernard,
Mishal Zohair,
Wiels Joëlle,
Tursz Thomas,
Busson Pierre
Publication year - 1999
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/(sici)1097-0215(19990517)81:4<645::aid-ijc22>3.0.co;2-0
Subject(s) - glycosphingolipid , nasopharyngeal carcinoma , tradd , traf2 , lymphoblast , epstein–barr virus , cancer research , immunoprecipitation , biology , signal transduction , antibody , microbiology and biotechnology , chemistry , virology , cell culture , virus , receptor , immunology , biochemistry , medicine , genetics , tumor necrosis factor receptor , apoptosis , programmed cell death , death domain , radiation therapy
Latent membrane protein 1 (LMP1) is an Epstein‐Barr virus (EBV) protein expressed in EBV‐transformed B lymphocytes and in approximately 50% of nasopharyngeal carcinomas (NPCs). LMP1 signaling involves several cellular signaling intermediates, especially TNF receptor–associated factors (TRAFs). We have shown previously that LMP1 is highly concentrated in a cell fraction called glycosphingolipid‐rich membrane complexes (GSL complexes). We report here that parallel accumulation of LMP1 and TRAF3, but not TRAF1 or TRADD, was observed in GSL complexes from lymphoblastoid and LMP1‐positive NPC cells. In contrast, TRAF3 was not concentrated in GSL complexes from LMP1‐negative cells. Binding of LMP1 and TRAF3 in GSL complexes was demonstrated in lymphoblastoid and NPC cells, by co‐immunoprecipitation with both anti‐LMP1 and anti‐TRAF3 antibodies. Int. J. Cancer 81:645–649, 1999. © 1999 Wiley‐Liss, Inc.