Open AccessExpression of Gamma Interferon-Dependent Genes Is Blocked Independently by Virion Host Shutoff RNase and by U S 3 Protein Kinase
Author(s) -
Li Liang,
Bernard Roizman
Publication year - 2008
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.02763-07
Subject(s) - biology , microbiology and biotechnology , interferon , protein kinase r , gene , mutant , rnase p , herpes simplex virus , protein kinase a , virus , gene expression , virology , phosphorylation , rna , cyclin dependent kinase 2 , biochemistry
Gamma interferon receptor α (IFN-γRα) 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-γRα is phosphorylated by the US 3 kinase. The modification is abolished in cells infected with ΔUS 3, ΔUL 13, or Δ(US 3/UL 13) mutant virus. Transcripts of the IFN-γ-dependent genes do not accumulate in cells transduced with the US 3 protein kinase and treated with IFN-γ. In contrast, the accumulation of IFN-γ-dependent gene transcripts is suppressed in cells infected with the wild-type virus, in cells infected with the ΔUS 3 mutant virus, and to a lesser extent in the ΔUL 41 virus-infected cells. The accumulation of IFN-γ-dependent gene transcripts in ΔUL 41-infected cells could be due at least in part to a significant delay and reduction in the accumulation of the US 3 protein. The results suggest that the expression of IFN-γ-dependent genes is blocked independently by the degradation of IFN-γ-dependent gene transcripts—a function of the virion host shutoff RNase—and by posttranslational modification of the IFN-γRα protein.