HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Thomas, C. Articles by Schwarzmann, F. Search for Related Content PubMed PubMed Citation Articles by Thomas, C. Articles by Schwarzmann, F. Agricola Articles by Thomas, C. Articles by Schwarzmann, F.

The BZLF1 promoter of Epstein–Barr virus is controlled by E box-/HI-motif-binding factors during virus latency

Cornelia Thomas

Institute for Medical Microbiology and Hygiene, University of Regensburg, Landshuter Strae 22, D-93047 Regensburg, Germany

Correspondence
Fritz Schwarzmann
fritz.schwarzmann{at}gmx.de

The BZLF1 open reading frame of Epstein–Barr virus (EBV) encodes an important transactivator of replication. During latency, transcription of this gene is switched off. HI motifs have been shown to cause negative regulation of the promoter. Using yeast one-hybrid assays, we isolated the E box-binding protein, E2-2, interacting with these motifs. Electrophoretic mobility shift assays demonstrated that E2-2 binds to HI, HI and HI, which contain E box consensus binding sites. Deletion of the HI-associated E boxes and overexpression of E2-2 in transfection assays revealed that these elements act as repressors in lymphoid cells. In contrast, in epithelial cells they contribute to the increased responsiveness of the promoter to transactivation by the BZLF1 protein. The data presented are in accord with an alternative and exclusive binding of different cell type- and differentiation-specific factors, such as E2-2, to the HI-associated E boxes in lymphoid and epithelial cells. This implies a role in cell type-specific virus replication.

Present address: MRC, Laboratory of Molecular Biology, Division of Protein and Nucleic Acid Chemistry, Cambridge, UK.

This article has been cited by other articles:

				J. Huang, G. Liao, H. Chen, F. Y. Wu, L. Hutt-Fletcher, G. S. Hayward, and S. D. Hayward Contribution of C/EBP Proteins to Epstein-Barr Virus Lytic Gene Expression and Replication in Epithelial Cells J. Virol., February 1, 2006; 80(3): 1098 - 1109. [Abstract] [Full Text] [PDF]