ArticlePloS one2012
Improper tagging of the non-essential small capsid protein VP26 impairs nuclear capsid egress of herpes simplex virus.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 36 citations in OpenAlex.
- A dual fluorescent herpes simplex virus type 1 recombinant reveals divergent outcomes of neuronal infection.Journal of virology · 2024Article
- Article
- Superinfection Exclusion of Alphaherpesviruses Interferes with Virion Trafficking.Microbiology spectrum · 2022Article
- Methods and Applications of Campenot Trichamber Neuronal Cultures for the Study of Neuroinvasive Viruses.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Correlative Light Electron Microscopy (CLEM) for Tracking and Imaging Viral Protein Associated Structures in Cryo-immobilized Cells.Journal of visualized experiments : JoVE · 2018Article
- Article
- Functional Carboxy-Terminal Fluorescent Protein Fusion to Pseudorabies Virus Small Capsid Protein VP26.Journal of virology · 2018Article
- Importin α1 is required for nuclear import of herpes simplex virus proteins and capsid assembly in fibroblasts and neurons.PLoS pathogens · 2018Article
- Inner tegument proteins of Herpes Simplex Virus are sufficient for intracellular capsid motility in neurons but not for axonal targeting.PLoS pathogens · 2017Article
- Visualization of herpes simplex virus type 1 virions using fluorescent colors.Journal of virological methods · 2017Article
- Visualizing Herpesvirus Procapsids in Living Cells.Journal of virology · 2016Article
- Dual-Color Herpesvirus Capsids Discriminate Inoculum from Progeny and Reveal Axonal Transport Dynamics.Journal of virology · 2016Article
- HSV1 MicroRNA Modulation of GPI Anchoring and Downstream Immune Evasion.Cell reports · 2016Article
- HVint: A Strategy for Identifying Novel Protein-Protein Interactions in Herpes Simplex Virus Type 1.Molecular & cellular proteomics : MCP · 2016Article
- Conserved Tryptophan Motifs in the Large Tegument Protein pUL36 Are Required for Efficient Secondary Envelopment of Herpes Simplex Virus Capsids.Journal of virology · 2016Article
- Article
- Review
- Remodeling nuclear architecture allows efficient transport of herpesvirus capsids by diffusion.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Function of the Herpes Simplex Virus 1 Small Capsid Protein VP26 Is Regulated by Phosphorylation at a Specific Site.Journal of virology · 2015Article
- DNA methyltransferase DNMT3A associates with viral proteins and impacts HSV-1 infection.Proteomics · 2015Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To analyze the subcellular trafficking of herpesvirus capsids, the small capsid protein has been labeled with different fluorescent proteins. Here, we analyzed the infectivity of several HSV1(17(+)) strains in which the N-terminal region of the non-essential small capsid protein VP26 had been tagged at different positions. While some variants replicated with similar kinetics as their parental wild type strain, others were not infectious at all. Improper tagging resulted in the aggregation of VP26 in the nucleus, prevented efficient nuclear egress of viral capsids, and thus virion formation. Correlative fluorescence and electron microscopy showed that these aggregates had sequestered several other viral proteins, but often did not contain viral capsids. The propensity for aggregate formation was influenced by the type of the fluorescent protein domain, the position of the inserted tag, the cell type, and the progression of infection. Among the tags that we have tested, mRFPVP26 had the lowest tendency to induce nuclear aggregates, and showed the least reduction in replication when compared to wild type. Our data suggest that bona fide monomeric fluorescent protein tags have less impact on proper assembly of HSV1 capsids and nuclear capsid egress than tags that tend to dimerize. Small chemical compounds capable of inducing aggregate formation of VP26 may lead to new antiviral drugs against HSV infections.
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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.