ArticleJournal of virology2001
Nuclear localization and shuttling of herpes simplex virus tegument protein VP13/14.
Article in Journal of virology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 69 citations in OpenAlex.
- The pUL47 tegument protein of Marek's Disease Virus interacts with p32/C1QBP to promote horizontal transmission.PLoS pathogens · 2025Article
- The functions of herpesvirus shuttling proteins in the virus lifecycle.Frontiers in microbiology · 2025Review
- Duck plague virus US3 protein kinase phosphorylates UL47 and regulates the subcellular localization of UL47.Frontiers in microbiology · 2022Article
- Pathogenesis and virulence of herpes simplex virus.Virulence · 2021Review
- Article
- "Non-Essential" Proteins of HSV-1 with Essential Roles In Vivo: A Comprehensive Review.Viruses · 2020Review
- Duck enteritis virus pUL47, as a late structural protein localized in the nucleus, mainly depends on residues 40 to 50 and 768 to 777 and inhibits IFN-β signalling by interacting with STAT1.Veterinary research · 2020Article
- Host shutoff activity of VHS and SOX-like proteins: role in viral survival and immune evasion.Virology journal · 2020Review
- Characterization of Nucleocytoplasmic Shuttling of Pseudorabies Virus Protein UL46.Frontiers in veterinary science · 2020Article
- Cellular Stress Response to Varicella-Zoster Virus Infection of Human Skin Includes Highly Elevated Interleukin-6 Expression.Open forum infectious diseases · 2018Article
- Infection and Transport of Herpes Simplex Virus Type 1 in Neurons: Role of the Cytoskeleton.Viruses · 2018Review
- Molecular characterization of duck enteritis virus UL41 protein.Virology journal · 2018Article
- Experimental Dissection of the Lytic Replication Cycles of Herpes Simplex VirusesFrontiers in microbiology · 2018Review
- Novel Structure and Unexpected RNA-Binding Ability of the C-Terminal Domain of Herpes Simplex Virus 1 Tegument Protein UL21.Journal of virology · 2016Article
- Review
- Role of Host Cell p32 in Herpes Simplex Virus 1 De-Envelopment during Viral Nuclear Egress.Journal of virology · 2015Article
- Herpes simplex virus 1 UL47 interacts with viral nuclear egress factors UL31, UL34, and Us3 and regulates viral nuclear egress.Journal of virology · 2014Article
- ORF11 protein interacts with the ORF9 essential tegument protein in varicella-zoster virus infection.Journal of virology · 2013Article
- Selective degradation of mRNAs by the HSV host shutoff RNase is regulated by the UL47 tegument protein.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Fluorescently tagged pUL47 of Marek's disease virus reveals differential tissue expression of the tegument protein in vivo.Journal of virology · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The herpes simplex virus type 1 gene UL47 encodes the tegument proteins referred to collectively as VP13/14, which are believed to be differentially modified forms of the same protein. Here we show that the major product of the UL47 gene during transient expression is VP14, suggesting that some feature of virus infection is required to produce VP13. We have tagged VP13/14 with green fluorescent protein and have demonstrated that the protein is targeted efficiently to the nucleus, where it often localizes in numerous punctate domains. Furthermore, we show that removal of the N-terminal 127 residues of the protein abrogates nuclear accumulation, and we have identified a 14-amino-acid peptide from this region that is sufficient to function as a nuclear targeting signal and transport a heterologous protein to the nucleus. This short peptide contains two runs of four arginine residues, suggesting that the VP13/14 nuclear localization signal may behave in a manner similar to that of the arginine-rich nuclear localization signals of the retrovirus transactivator proteins Tat, Rev, and Rex. In addition, by using heterokaryon assays, we show that VP13/14 is capable of shuttling between the nucleus and cytoplasm of the cell, a property that may be attributed to three leucine-rich stretches in the C-terminal half of the protein that again bear similarity to the nuclear export signals of Rev and Rex. This is the first demonstration of a tegument protein that is specifically targeted to the nucleus, a feature which may be relevant both during virus entry, when VP13/14 enters the cell as a component of the tegument, and at later times, when large amounts of newly synthesized VP13/14 are present within the cell.
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