ArticleVirology2008
Sequences in the UL11 tegument protein of herpes simplex virus that control association with detergent-resistant membranes.
Article in Virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 28 citations in OpenAlex.
- Features and Functions of the Conserved Herpesvirus Tegument Protein UL11 and Its Binding Partners.Frontiers in microbiology · 2022Review
- "Non-Essential" Proteins of HSV-1 with Essential Roles In Vivo: A Comprehensive Review.Viruses · 2020Review
- Article
- Domain Interaction Studies of Herpes Simplex Virus 1 Tegument Protein UL16 Reveal Its Interaction with Mitochondria.Journal of virology · 2017Article
- The herpes simplex virus 1 UL51 protein interacts with the UL7 protein and plays a role in its recruitment into the virion.Journal of virology · 2015Article
- Herpes simplex virus 1 glycoprotein M and the membrane-associated protein UL11 are required for virus-induced cell fusion and efficient virus entry.Journal of virology · 2013Article
- Function of glycoprotein E of herpes simplex virus requires coordinated assembly of three tegument proteins on its cytoplasmic tail.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Regulated interaction of tegument proteins UL16 and UL11 from herpes simplex virus.Journal of virology · 2012Article
- Characterization and intracellular trafficking of Epstein-Barr virus BBLF1, a protein involved in virion maturation.Journal of virology · 2012Article
- Direct and specific binding of the UL16 tegument protein of herpes simplex virus to the cytoplasmic tail of glycoprotein E.Journal of virology · 2011Article
- Interaction and interdependent packaging of tegument protein UL11 and glycoprotein e of herpes simplex virus.Journal of virology · 2011Article
- Expression and characterization of UL16 gene from duck enteritis virus.Virology journal · 2011Article
- Sequence variability in clinical and laboratory isolates of herpes simplex virus 1 reveals new mutations.Journal of virology · 2010Article
- Complex mechanisms for the packaging of the UL16 tegument protein into herpes simplex virus.Virology · 2010Article
- Interaction domains of the UL16 and UL21 tegument proteins of herpes simplex virus.Journal of virology · 2010Article
- Article
- Analysis of the interaction between the UL11 and UL16 tegument proteins of herpes simplex virus.Journal of virology · 2008Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The product of the UL11 gene of HSV-1 is a small, membrane-bound tegument protein with features that are conserved among all herpesviruses. For all viruses examined, mutants lacking this protein (or its homolog) have budding defects and accumulate capsids in the cytoplasm of the infected cell. UL11 binds to the cytoplasmic faces of host membranes via N-terminal myristate and nearby palmitate moieties. These fatty-acid modifications are typical of proteins that localize to detergent-resistant membranes (DRMs), and the experiments described here revealed that a small amount (approximately 10%) of UL11 retains the ability to float in sucrose gradients following treatment of cells with Triton X-100. However, mutants lacking sequences previously shown to be involved in the trafficking of UL11 from the plasma membrane (LI and acidic cluster motifs) were found to have a dramatically increased association with DRMs. These findings emphasize the dynamic properties of this poorly-understood but conserved tegument protein.
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Registered trials
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