title: Functional interactions between the Epstein-Barr virus BZLF1 protein and the promyelocytic leukemia protein.
abstract: The Epstein-Barr virus immediate-early protein BZLF1 (Z) has been shown to alter the cellular localization of the promyelocytic leukemia (PML) protein. PML has important implications for growth control, apoptosis, anti-viral effects and many more processes. Here we further examined the relationship between PML and the Epstein-Barr virus Z protein. We examined the effect of Z expression on PML protein levels, and the effect of increased PML protein levels on Z-mediated dispersion of PML bodies. We found that increased levels of PML protein, such as through interferon treatment, were able to suppress Z-mediated PML body dispersion. We also studied the consequences of PML dispersion by Z, by examining p21 transactivation, A20 transactivation, and MHC Class I presentation levels in Z-expressing cells. We found that, while Z-mediated dispersion of PML did not affect MHC Class I presentation, it did alter p21 and A20 expression. In addition, we found that increased levels of PML were able to prevent Z protein binding to mitotic chromosomes. Our work implies that the balance of PML and Z levels in cells may affect how each protein functions.
authors.affiliation: Department of Biology, University of North Carolina at Greensboro, Greensboro, NC 27402, USA.
authors.forename: Brandy L
authors.initials: BL
authors.lastname: Bowling
authors.forename: Amy L
authors.initials: AL
authors.lastname: Adamson
mesh_terms: D019677:Artificial Gene Fusion; D015153:Blotting, Western; D002875:Chromosomes / Q000737:chemistry; D004268:DNA-Binding Proteins / Q000378:metabolism*; D015870:Gene Expression; D017930:Genes, Reporter; D006367:HeLa Cells; D015395:Histocompatibility Antigens Class I / Q000502:physiology; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins; D008156:Luciferases / Q000032:analysis / Q000235:genetics; D018613:Microscopy, Confocal; D008856:Microscopy, Fluorescence; D009363:Neoplasm Proteins / Q000378:metabolism*; D009687:Nuclear Proteins / Q000378:metabolism*; D000071156:Promyelocytic Leukemia Protein; D011485:Protein Binding; D011506:Proteins / Q000032:analysis; D015534:Trans-Activators / Q000378:metabolism*; D014157:Transcription Factors / Q000378:metabolism*; D015533:Transcriptional Activation; D000072598:Tumor Necrosis Factor alpha-Induced Protein 3; D025521:Tumor Suppressor Proteins / Q000032:analysis / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism*
chemical_list: C063676:BZLF1 protein, Herpesvirus 4, Human; D004268:DNA-Binding Proteins; D015395:Histocompatibility Antigens Class I; D047908:Intracellular Signaling Peptides and Proteins; D009363:Neoplasm Proteins; D009687:Nuclear Proteins; D000071156:Promyelocytic Leukemia Protein; D011506:Proteins; D015534:Trans-Activators; D014157:Transcription Factors; D025521:Tumor Suppressor Proteins; D014764:Viral Proteins; C070576:PML protein, human; D008156:Luciferases; C076529:TNFAIP3 protein, human; D000072598:Tumor Necrosis Factor alpha-Induced Protein 3