Abstract：
:ICP27 is an essential herpes simplex virus type 1 (HSV-1) nuclear protein which regulates viral early and late genes during infection. The exact mechanism by which ICP27 modulates viral gene expression is unknown, but considerable evidence suggests that it functions posttranscriptionally. In this study, we have asked whether ICP27, like some other viral and cellular posttranscriptional regulatory proteins, shuttles between the nuclear and cytoplasmic compartments of the cell. Using an interspecies heterokaryon assay, we demonstrate that ICP27, but not the HSV-1 nuclear proteins ICP4 or ICP8, is an efficient shuttling protein. ICP27's shuttling ability does not depend on viral infection or other HSV-1 proteins, as it shuttles even when transiently expressed in uninfected cells. To understand the importance of shuttling for ICP27's regulatory functions, we examined several mutant forms of ICP27 to see whether they exhibited altered shuttling. We identified three ICP27 mutations which partially disrupt shuttling, as well as one mutation, M15, which completely abrogates this activity. The M15 mutation alters residues 465 and 466 near the carboxyl terminus of ICP27 and was previously shown to inactivate ICP27's ability to induce certain viral late mRNAs. These results suggest that ICP27's nuclear shuttling activity is involved in its viral late gene activation function.
journal_name
Virologyjournal_title
Virologyauthors
Mears WE,Rice SAdoi
10.1006/viro.1997.9006subject
Has Abstractpub_date
1998-03-01 00:00:00pages
128-37issue
1eissn
0042-6822issn
1096-0341pii
S0042-6822(97)99006-1journal_volume
242pub_type
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