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Expression profiling of host genes modulated by Epstein-Barr virus (EBV) Rta in HEK293 cells

ABSTRACT: EBV Rta is a transcriptional activator that functions to disrupt EBV latency in cells of epithelial origin. This series of experiment is to identify host genes that are moduated by the expression of doxycycline-inducible EBV Rta in HEK293 cells. Designations for the pooled EBV Rta inducible cell lines is 293TetER; pooled luciferase inducible lines is 293TetLuc (control). Overall design: Both 293TetER and 293TetLuc cells were grown to log-phase before doxycycline induction. Same number of cells from the two cell lines were treated with doxycycline for 48 h. Experiments were performed in duplicates. Total RNAs from the four samples were extracted and subjected to microarray analysis (Affymetrix Human Gene 1.0 ST Array , n=33,297). Compared to doxycycline treated 293TetLuc, we sought to identify genes up- or down-regulated in by EBV Rta in doxycycline treated 293TetER cells..

INSTRUMENT(S): [HuGene-1_0-st] Affymetrix Human Gene 1.0 ST Array [transcript (gene) version]

ORGANISM(S): Homo sapiens

SUBMITTER: Su-Fang Lin

PROVIDER: GSE24585 | GEO | 2011-05-22

SECONDARY ACCESSION(S): PRJNA133583

REPOSITORIES: GEO

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			Action	DRS
	GSE24585_Fold_chg.txt.gz	Txt
	GSE24585_RAW.tar	Raw
	filelist.txt	Txt

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Project description:Kaposi's sarcoma-associated herpesvirus (KSHV) is a human gammaherpesvirus that has been implicated in the pathogenesis of Kaposi's sarcoma and B-cell neoplasms. The genomic organization of KSHV is similar to that of Epstein-Barr virus (EBV). EBV encodes two transcriptional factors, Rta and Zta, which functionally interact to transactivate EBV genes during replication and reactivation from latency. KSHV encodes a basic leucine zipper protein (K-bZIP), a homologue of EBV Zta, and K-Rta, the homologue of EBV Rta. EBV Rta and Zta are strong transcriptional transactivators. Although there is ample evidence that K-Rta is a potent transactivator, the role of K-bZIP as a transcriptional factor is much less clear. In this study, we report that K-bZIP modulates K-Rta function. We show that K-bZIP directly interacts with K-Rta in vivo and in vitro. This association is specific, requiring the basic domain (amino acids 122 to 189) of K-bZIP and a specific region (amino acids 499 to 550) of K-Rta, and can be detected with K-bZIP and K-Rta endogenously expressed in BCBL-1 cells treated with tetradecanoyl phorbol acetate. The functional relevance of this association was revealed by the observation that K-bZIP represses the transactivation of the ORF57 promoter by K-Rta in a dose-dependent manner. K-bZIP lacking the interaction domain fails to repress K-Rta-mediated transactivation; this finding attests to the specificity of the repression. Interestingly, this repression is not observed for the promoter of polyadenylated nuclear (PAN) RNA, another target of K-Rta; thus, repression is promoter dependent. Finally, we provide evidence that the modulation of K-Rta by K-bZIP also occurs in vivo during reactivation of the viral genome in BCBL-1 cells. When K-bZIP is overexpressed in BCBL-1 cells, the level of expression of ORF57 but not PAN RNA is repressed. These data support the model that one function of K-bZIP is to modulate the activity of the transcriptional transactivator K-Rta.

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Expression profiling of host genes modulated by Epstein-Barr virus (EBV) Rta in HEK293 cells

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