ArticleJournal of virology2005
Control of VP16 translation by the herpes simplex virus type 1 immediate-early protein ICP27.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Herpes Simplex Virus-1 ICP27 Nuclear Export Signal Mutants Exhibit Cell Type-Dependent Deficits in Replication and ICP4 Expression.Journal of virology · 2023Article
- Deletion of Double Copies of the US1 Gene Reduces the Infectivity of Recombinant Duck Plague VirusMicrobiology spectrum · 2022Article
- Preventing translational inhibition from ribosomal protein insufficiency by a herpes simplex virus-encoded ribosome-associated protein.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- TheJournal of virology · 2019Article
- Article
- Cellular Cholesterol Facilitates the Postentry Replication Cycle of Herpes Simplex Virus 1.Journal of virology · 2017Article
- Viral and cellular mRNA-specific activators harness PABP and eIF4G to promote translation initiation downstream of cap binding.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Regulation of viral gene expression by duck enteritis virus UL54.Scientific reports · 2017Article
- Duck enteritis virus UL54 is an IE protein primarily located in the nucleus.Virology journal · 2015Article
- Modulation of the Translational Landscape During Herpesvirus Infection.Annual review of virology · 2015Review
- Functional comparison of herpes simplex virus 1 (HSV-1) and HSV-2 ICP27 homologs reveals a role for ICP27 in virion release.Journal of virology · 2015Article
- The herpes simplex virus 2 virion-associated ribonuclease vhs interferes with stress granule formation.Journal of virology · 2014Article
- Tinkering with translation: protein synthesis in virus-infected cells.Cold Spring Harbor perspectives in biology · 2013Review
- mRNA decay during herpes simplex virus (HSV) infections: mutations that affect translation of an mRNA influence the sites at which it is cleaved by the HSV virion host shutoff (Vhs) protein.Journal of virology · 2013Article
- Herpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through Nup62, inhibiting host nucleocytoplasmic transport pathways.The Journal of biological chemistry · 2012Article
- Deciphering novel host-herpesvirus interactions by virion proteomics.Frontiers in microbiology · 2012Article
- Role of herpes simplex virus ICP27 in the degradation of mRNA by virion host shutoff RNase.Journal of virology · 2010Article
- Poly(A)-binding protein 1 partially relocalizes to the nucleus during herpes simplex virus type 1 infection in an ICP27-independent manner and does not inhibit virus replication.Journal of virology · 2010Article
- Three arginine residues within the RGG box are crucial for ICP27 binding to herpes simplex virus 1 GC-rich sequences and for efficient viral RNA export.Journal of virology · 2010Article
- Herpes simplex virus 1 regulatory protein ICP27 undergoes a head-to-tail intramolecular interaction.Journal of virology · 2010Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Herpes simplex virus (HSV) ICP27 is an essential and multifunctional regulator of gene expression that modulates the synthesis and maturation of viral and cellular mRNAs. Processes that are affected by ICP27 include transcription, pre-mRNA splicing, polyadenylation, and nuclear RNA export. We have examined how ICP27 influences the expression of the essential HSV tegument protein and transactivator of immediate-early gene expression VP16. We monitored the effects of ICP27 on the levels, nuclear export, and polyribosomal association of VP16 mRNA and on the amount and stability of VP16 protein. Deletion of ICP27 reduced the levels of VP16 mRNA without altering its nuclear export or the stability of the encoded protein. However, the translational yield of the VP16 mRNA produced in the absence of ICP27 was reduced 9- to 80-fold relative to that for wild-type infection, suggesting a defect in translation. In the absence of ICP27, the majority of cytoplasmic VP16 mRNA was not associated with actively translating polyribosomes but instead cosedimented with 40S ribosomal subunits, indicating that the translational defect is likely at the level of initiation. These effects were mRNA specific, as polyribosomal analysis of two cellular transcripts (glyceraldehyde-3-phosphate dehydrogenase and beta-actin) and two early HSV transcripts (thymidine kinase and ICP8) indicated that ICP27 is not required for efficient translation of these mRNAs. Thus, we have uncovered a novel mRNA-specific translational regulatory function of ICP27.
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