ArticlePLoS pathogens2018
Importin α1 is required for nuclear import of herpes simplex virus proteins and capsid assembly in fibroblasts and neurons.
Article in PLoS pathogens, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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32 citing papers in PubMed, 54 citations in OpenAlex.
- The antiviral GTPase MxB is packaged into virions and binds via its N-terminal domain to alphaherpesvirus capsids.PLoS pathogens · 2026Article
- Exploring EBNA3C Genetic Variability and Recombination in Epstein-Barr Virus-Associated Cancers.International journal of molecular sciences · 2026Article
- Alpha-Actinin-3 Deficiency Links Genetic Susceptibility to Renal Fibrosis: Evidence From Hemodialysis Patients and Murine Models.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- Importinα3 Mediates BmNPV Nucleocapsid Nuclear Entry via a Ran-Independent Pathway.Current microbiology · 2025Article
- Herpes simplex virus assembly and spread in murine skin after infection from the outside.Journal of virology · 2025Article
- Review
- Control of HSV-1 Infection: Directions for the Development of CRISPR/Cas-Based Therapeutics and Diagnostics.International journal of molecular sciences · 2024Review
- Article
- Article
- A functional and structural comparative analysis of large tumor antigens reveals evolution of different importin α-dependent nuclear localization signals.Protein science : a publication of the Protein Society · 2024Article
- Helical reconstruction of VP39 reveals principles for baculovirus nucleocapsid assembly.Nature communications · 2024Article
- Communicating pain: emerging axonal signaling in peripheral neuropathic pain.Frontiers in neuroanatomy · 2024Review
- GARP and EARP are required for efficient BoHV-1 replication as identified by a genome wide CRISPR knockout screen.PLoS pathogens · 2023Article
- Synergistic In Vitro Antiviral Effect of Combinations of Ivermectin, Essential Oils, and 18-(Phthalimid-2-yl)ferruginol against Arboviruses and Herpesvirus.Pharmaceuticals (Basel, Switzerland) · 2023Article
- Helical reconstruction of VP39 reveals principles for baculovirus nucleocapsid assembly.bioRxiv : the preprint server for biology · 2023Article
- Role of Innate Interferon Responses at the Ocular Surface in Herpes Simplex Virus-1-Induced Herpetic Stromal Keratitis.Pathogens (Basel, Switzerland) · 2023Review
- Review
- The interferon-inducible GTPase MxB promotes capsid disassembly and genome release of herpesviruses.eLife · 2022Article
- Dual RNA-Seq of H5N1 Avian Influenza Virus and Host Cell Transcriptomes Reveals Novel Insights Into Host-Pathogen Cross Talk.Frontiers in microbiology · 2022Article
- Pathogenesis and virulence of herpes simplex virus.Virulence · 2021Review
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Authors and funding
18 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Herpesviruses are large DNA viruses which depend on many nuclear functions, and therefore on host transport factors to ensure specific nuclear import of viral and host components. While some import cargoes bind directly to certain transport factors, most recruit importin β1 via importin α. We identified importin α1 in a small targeted siRNA screen to be important for herpes simplex virus (HSV-1) gene expression. Production of infectious virions was delayed in the absence of importin α1, but not in cells lacking importin α3 or importin α4. While nuclear targeting of the incoming capsids, of the HSV-1 transcription activator VP16, and of the viral genomes were not affected, the nuclear import of the HSV-1 proteins ICP4 and ICP0, required for efficient viral transcription, and of ICP8 and pUL42, necessary for DNA replication, were reduced. Furthermore, quantitative electron microscopy showed that fibroblasts lacking importin α1 contained overall fewer nuclear capsids, but an increased proportion of mature nuclear capsids indicating that capsid formation and capsid egress into the cytoplasm were impaired. In neurons, importin α1 was also not required for nuclear targeting of incoming capsids, but for nuclear import of ICP4 and for the formation of nuclear capsid assembly compartments. Our data suggest that importin α1 is specifically required for the nuclear localization of several important HSV1 proteins, capsid assembly, and capsid egress into the cytoplasm, and may become rate limiting in situ upon infection at low multiplicity or in terminally differentiated cells such as neurons.
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