ArticleJournal of virology2007
The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins.
Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
97 citing papers in PubMed, 134 citations in OpenAlex.
- Tethered release of the pseudorabies virus deubiquitinase from the capsid promotes enzymatic activity.Journal of virology · 2025Article
- Article
- Molecular plasticity of herpesvirus nuclear egress analysed in situ.Nature microbiology · 2024Article
- The VP1/2 Protein of a New Recombinant PRV Strain Promotes the Infectivity and Pathogenicity of PRV in Northeastern China.Transboundary and emerging diseases · 2024Article
- Review
- Proteomic Comparison of Three Wild-Type Pseudorabies Virus Strains and the Attenuated Bartha Strain Reveals Reduced Incorporation of Several Tegument Proteins in Bartha Virions.Journal of virology · 2022Article
- The interferon-inducible GTPase MxB promotes capsid disassembly and genome release of herpesviruses.eLife · 2022Article
- Motor Skills: Recruitment of Kinesins, Myosins and Dynein during Assembly and Egress of Alphaherpesviruses.Viruses · 2021Review
- Engagement of Neurotropic Viruses in Fast Axonal Transport: Mechanisms, Potential Role of Host Kinases and Implications for Neuronal Dysfunction.Frontiers in cellular neuroscience · 2021Article
- The Role of VP16 in the Life Cycle of Alphaherpesviruses.Frontiers in microbiology · 2020Review
- Microtubule-Dependent Trafficking of Alphaherpesviruses in the Nervous System: The Ins and Outs.Viruses · 2019Review
- The Herpes Simplex Virus 1 Deamidase Enhances Propagation but Is Dispensable for Retrograde Axonal Transport into the Nervous System.Journal of virology · 2019Article
- Qualitative Differences in Capsidless L-Particles Released as a By-Product of Bovine Herpesvirus 1 and Herpes Simplex Virus 1 Infections.Journal of virology · 2018Article
- The Apical Region of the Herpes Simplex Virus Major Capsid Protein Promotes Capsid Maturation.Journal of virology · 2018Article
- Structure of the herpes simplex virus type 2 C-capsid with capsid-vertex-specific component.Nature communications · 2018Article
- Dissecting the Herpesvirus Architecture by Targeted Proteolysis.Journal of virology · 2018Article
- Structure of the herpes simplex virus 1 capsid with associated tegument protein complexes.Science (New York, N.Y.) · 2018Article
- Experimental Dissection of the Lytic Replication Cycles of Herpes Simplex VirusesFrontiers in microbiology · 2018Review
- The pUL37 tegument protein guides alpha-herpesvirus retrograde axonal transport to promote neuroinvasion.PLoS pathogens · 2017Article
- A pUL25 dimer interfaces the pseudorabies virus capsid and tegument.The Journal of general virology · 2017Article
37 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
How alphaherpesvirus capsids acquire tegument proteins remains a key question in viral assembly. Using pseudorabies virus (PRV), we have previously shown that the 62 carboxy-terminal amino acids of the VP1/2 large tegument protein are essential for viral propagation and when transiently expressed as a fusion to green fluorescent protein relocalize to nuclear capsid assemblons following viral infection. Here, we show that localization of the VP1/2 capsid-binding domain (VP1/2cbd) into assemblons is conserved in herpes simplex virus type 1 (HSV-1) and that this recruitment is specifically on capsids. Using a mutant virus screen, we find that the protein product of the UL25 gene is essential for VP1/2cbd association with capsids. An interaction between UL25 and VP1/2 was corroborated by coimmunoprecipitation from cells transiently expressing either HSV-1 or PRV proteins. Taken together, these findings suggest that the essential function of the VP1/2 carboxy terminus is to anchor the VP1/2 tegument protein to capsids. Furthermore, UL25 encodes a multifunctional capsid protein involved in not only encapsidation, as previously described, but also tegumentation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.