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Vol. 12, No. 13, pp. 2061-2072, July 1, 1998
1 Department of Pathology, Harvard Medical School,
Boston, Massachusetts 02115 USA;
2 Harvard Medical School
and Massachusetts General Hospital Cancer Center,
Charlestown, Massachusetts 02129 USA
Interferon regulatory factor-3 (IRF-3) was found to specifically
interact with HPV16 E6 in a yeast two-hybrid screen. IRF-3 is activated
by the presence of double-stranded RNA or by virus infection to form a
stable complex with other transcriptional regulators that bind to the
regulatory elements of the IFN
promoter. We show that IRF-3 is a
potent transcriptional activator and demonstrate that HPV16 E6 can
inhibit its transactivation function. The expression of HPV16 E6 in
primary human keratinocytes inhibits the induction of IFN mRNA
following Sendai virus infection. The binding of HPV16 E6 to IRF-3 does
not result in its ubiquitination or degradation. We propose that the
interaction of E6 with IRF-3 and the inhibition of IRF-3's
transcriptional activity may provide the virus a means to circumvent
the normal antiviral response of an HPV16-infected cell.
[Key Words: IRF-3; HPV16; transcription; protein-protein interactions; oncoprotein]
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