ArticleJournal of virology2002
Sequential localization of two herpes simplex virus tegument proteins to punctate nuclear dots adjacent to ICP0 domains.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Article
- Cell-to-cell transmission of HSV1 in human keratinocytes in the absence of the major entry receptor, nectin1.PLoS pathogens · 2021Article
- Characterization of Nucleocytoplasmic Shuttling of Pseudorabies Virus Protein UL46.Frontiers in veterinary science · 2020Article
- Alphaherpesvirus Major Tegument Protein VP22: Its Precise Function in the Viral Life Cycle.Frontiers in microbiology · 2020Review
- Article
- Visualization of herpes simplex virus type 1 virions using fluorescent colors.Journal of virological methods · 2017Article
- Spatial and Temporal Resolution of Global Protein Synthesis during HSV Infection Using Bioorthogonal Precursors and Click Chemistry.PLoS pathogens · 2016Article
- HSV-1 Glycoproteins Are Delivered to Virus Assembly Sites Through Dynamin-Dependent Endocytosis.Traffic (Copenhagen, Denmark) · 2016Article
- Review
- DNA virus replication compartments.Journal of virology · 2014Review
- A single gD glycoprotein can mediate infection by Herpes simplex virus.Journal of the American Chemical Society · 2013Article
- Fluorosomes: fluorescent virus-like nanoparticles that represent a convenient tool to visualize receptor-ligand interactions.Sensors (Basel, Switzerland) · 2013Review
- Virus-induced aggregates in infected cells.Viruses · 2012Review
- Article
- Recruitment of herpes simplex virus type 1 immediate-early protein ICP0 to the virus particle.Journal of virology · 2010Article
- Article
- Identification of a highly conserved, functional nuclear localization signal within the N-terminal region of herpes simplex virus type 1 VP1-2 tegument protein.Journal of virology · 2008Article
- The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins.Journal of virology · 2007Article
- Two-color fluorescence analysis of individual virions determines the distribution of the copy number of proteins in herpes simplex virus particles.Biophysical journal · 2007Article
- A guide to viral inclusions, membrane rearrangements, factories, and viroplasm produced during virus replication.Advances in virus research · 2007Review
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The subcellular localization of herpes simplex virus tegument proteins during infection is varied and complex. By using viruses expressing tegument proteins tagged with fluorescent proteins, we previously demonstrated that the major tegument protein VP22 exhibits a cytoplasmic localization, whereas the major tegument protein VP13/14 localizes to nuclear replication compartments and punctate domains. Here, we demonstrate the presence of a second minor population of VP22 in nuclear dots similar in appearance to those formed by VP13/14. We have constructed the first-described doubly fluorescence-tagged virus expressing VP22 and VP13/14 as fusion proteins with cyan fluorescent protein and yellow fluorescent protein, respectively. Visualization of both proteins within the same live infected cells has indicated that these two tegument proteins localize to the same nuclear dots but that VP22 appears there earlier than VP13/14. Further studies have shown that these tegument-specific dots are detectable as phase-dense bodies as early as 2 h after infection and that they are different from the previously described nuclear domains that contain capsid proteins. They are also different from the ICP0 domains formed at cellular nuclear domain 10 sites early in infection but, in almost all cases, are located in juxtaposition to these ICP0 domains. Hence, these tegument proteins join a growing number of proteins that are targeted to discrete nuclear domains in the herpesvirus-infected cell nucleus.
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