ArticleJournal of virology2006
The amino terminus of the herpes simplex virus 1 protein Vhs mediates membrane association and tegument incorporation.
Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- Herpes Simplex Virus Capsid Localization to ESCRT-VPS4 Complexes in the Presence and Absence of the Large Tegument Protein UL36p.Journal of virology · 2016Article
- Herpes Simplex Virus Capsid-Organelle Association in the Absence of the Large Tegument Protein UL36p.Journal of virology · 2015Article
- Deletion of the herpes simplex virus 1 UL49 gene results in mRNA and protein translation defects that are complemented by secondary mutations in UL41.Journal of virology · 2012Article
- Article
- Time-dependent transformation of the herpesvirus tegument.Journal of virology · 2009Article
- Characterization of subcellular localization of duck enteritis virus UL51 protein.Virology journal · 2009Article
- UL36p is required for efficient transport of membrane-associated herpes simplex virus type 1 along microtubules.Journal of virology · 2008Article
- Selective ablation of virion host shutoff protein RNase activity attenuates herpes simplex virus 2 in mice.Journal of virology · 2008Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Assembly of herpes simplex viruses (HSV) is a poorly understood process involving multiple redundant interactions between large number of tegument and envelope proteins. We have previously shown (G. E. Lee, G. A. Church, and D. W. Wilson, J. Virol. 77:2038-2045, 2003) that the virion host shutoff (Vhs) tegument protein is largely insoluble in HSV-infected cells and is also stably associated with membranes. Here we demonstrate that both insolubility and stable membrane binding are stimulated during the course of an HSV infection. Furthermore, we have found that the amino-terminal 42 residues of Vhs are sufficient to mediate membrane association and tegument incorporation when fused to a green fluorescent protein (GFP) reporter. Particle incorporation correlates with sorting to cytoplasmic punctate structures that may correspond to sites of HSV assembly. We conclude that the amino terminus of Vhs mediates targeting to sites of HSV assembly and to the viral tegument.
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Registered trials
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