ArticleJournal of virology2009
Varicella-zoster virus immediate-early 63 protein interacts with human antisilencing function 1 protein and alters its ability to bind histones h3.1 and h3.3.
Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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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Who cites it
25 citing papers in PubMed, 48 citations in OpenAlex.
- Daxx and HIRA go viral - How chromatin remodeling complexes affect DNA virus infection.Tumour virus research · 2025Review
- Neurotropic Viruses as Acute and Insidious Drivers of Aging.Biomolecules · 2025Review
- Virus-Host Protein Interaction Network of the Hepatitis E Virus ORF2-4 by Mammalian Two-Hybrid Assays.Viruses · 2023Article
- Multifaceted Roles of ICP22/ORF63 Proteins in the Life Cycle of Human Herpesviruses.Frontiers in microbiology · 2021Review
- Simian varicella virus causes robust transcriptional changes in T cells that support viral replication.Virus research · 2017Article
- Varicella zoster virus infection of human fetal lung cells alters mitochondrial morphology.Journal of neurovirology · 2016Article
- Identification of small molecules that inhibit the histone chaperone Asf1 and its chromatin function.BMB reports · 2015Article
- Varicella zoster virus infection.Nature reviews. Disease primers · 2015Review
- A comparison of herpes simplex virus type 1 and varicella-zoster virus latency and reactivation.The Journal of general virology · 2015Review
- An in vitro model of latency and reactivation of varicella zoster virus in human stem cell-derived neurons.PLoS pathogens · 2015Article
- Pathogens hijack the epigenome: a new twist on host-pathogen interactions.The American journal of pathology · 2014Review
- Activation of H2AX and ATM in varicella-zoster virus (VZV)-infected cells is associated with expression of specific VZV genes.Virology · 2014Article
- Varicella-zoster.Handbook of clinical neurology · 2014Review
- Chromatin assembly on herpes simplex virus 1 DNA early during a lytic infection is Asf1a dependent.Journal of virology · 2012Article
- Herpes simplex virus and varicella zoster virus, the house guests who never leave.Herpesviridae · 2012Article
- Recombinant monoclonal antibody recognizes a unique epitope on varicella-zoster virus immediate-early 63 protein.Journal of virology · 2012Article
- Dynamic association of gammaherpesvirus DNA with core histone during de novo lytic infection of primary cells.Virology · 2011Article
- Varicella zoster virus-induced pain and post-herpetic neuralgia in the human host and in rodent animal models.Journal of neurovirology · 2011Article
- Varicella zoster virus (VZV) infects and establishes latency in enteric neurons.Journal of neurovirology · 2011Article
- Simian varicella virus open reading frame 63/70 expression is required for efficient virus replication in culture.Journal of neurovirology · 2011Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Varicella-zoster virus (VZV) immediate-early 63 protein (IE63) is abundantly expressed during both acute infection in vitro and latent infection in human ganglia. Using the yeast two-hybrid system, we found that VZV IE63 interacts with human antisilencing function 1 protein (ASF1). ASF1 is a nucleosome assembly factor which is a member of the H3/H4 family of histone chaperones. IE63 coimmunoprecipitated and colocalized with ASF1 in transfected cells expressing IE63 and in VZV-infected cells. IE63 also colocalized with ASF1 in both lytic and latently VZV-infected enteric neurons. ASF1 exists in two isoforms, ASF1a and ASF1b, in mammalian cells. IE63 preferentially bound to ASF1a, and the amino-terminal 30 amino acids of ASF1a were critical for its interaction with IE63. VZV IE63 amino acids 171 to 208 and putative phosphorylation sites of IE63, both of which are critical for virus replication and latency in rodents, were important for the interaction of IE63 with ASF1. Finally, we found that IE63 increased the binding of ASF1 to histone H3.1 and H3.3, which suggests that IE63 may help to regulate levels of histones in virus-infected cells. Since ASF1 mediates eviction and deposition of histones during transcription, the interaction of VZV IE63 with ASF1 may help to regulate transcription of viral or cellular genes during lytic and/or latent infection.
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