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An activation-defective mutant of the human cytomegalovirus IE2p86 protein inhibits NF-B-mediated stimulation of the human interleukin-6 promoter

Vicky Dickinson^1,

¹ Cardiff School of Biosciences, Cardiff University, Cardiff CF10 3US, UK
² Department of Microbiology, Carver College of Medicine, University of Iowa, Iowa City, IA 52242, USA

Correspondence
Richard Caswell
CaswellR{at}cf.ac.uk

The IE2p86 protein of human cytomegalovirus is an essential activator of early- and late-phase viral gene expression. Whilst IE2p86 activates expression of a number of cellular genes, it also represses certain cellular genes, particularly those activated by nuclear factor B (NF-B). As the interleukin-6 (IL-6) promoter can be activated by both NF-B and IE2p86, it was examined whether there is competition between these two factors. Here, it is reported that both wild-type and mutant IE2p86 can block activation of the IL-6 promoter in response to interleukin-1. By using an artificial activator in which the activation domain of NF-B is directed to the promoter by the GAL4 DNA-binding domain, it is shown that the mutant form of IE2p86 can inhibit NF-B-mediated activation at a step subsequent to promoter recruitment. These data therefore suggest a novel mechanism for inhibition of NF-B by IE2p86.

Deceased.

Supplementary figures showing binding of IE2p86 and CAD291 to basal transcription factors in vitro and the sequence of the human IL-6 promoter are available with the online version of this paper.

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