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Journal of Virology, May 2008, p. 4688-4696, Vol. 82, No. 10
0022-538X/08/$08.00+0 doi:10.1128/JVI.02763-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Marjorie B. Kovler Viral Oncology Laboratories, The University of Chicago, 910 East 58th Street, Chicago, Illinois 60637
Received 30 December 2007/ Accepted 28 February 2008
Gamma interferon receptor
(IFN-
R
) is stable but posttranslationally modified in herpes simplex virus 1(F) [HSV-1(F)]-infected cells. Studies with antibody directed to the phosphorylation site indicate that IFN-
R
is phosphorylated by the US3 kinase. The modification is abolished in cells infected with
US3,
UL13, or
(US3/UL13) mutant virus. Transcripts of the IFN-
-dependent genes do not accumulate in cells transduced with the US3 protein kinase and treated with IFN-
. In contrast, the accumulation of IFN-
-dependent gene transcripts is suppressed in cells infected with the wild-type virus, in cells infected with the
US3 mutant virus, and to a lesser extent in the
UL41 virus-infected cells. The accumulation of IFN-
-dependent gene transcripts in
UL41-infected cells could be due at least in part to a significant delay and reduction in the accumulation of the US3 protein. The results suggest that the expression of IFN-
-dependent genes is blocked independently by the degradation of IFN-
-dependent gene transcripts—a function of the virion host shutoff RNase—and by posttranslational modification of the IFN-
R
protein.
Published ahead of print on 5 March 2008.
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