ArticleNature communications2014
Membrane deformation and scission by the HSV-1 nuclear egress complex.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.
What it found
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Who cites it
106 citing papers in PubMed.
- Conserved assembly architecture of the essential herpesvirus packaging accessory factor.PLoS pathogens · 2026Article
- The MHV-68 nuclear egress complex supports C-capsid selective capsid egress.Journal of virology · 2026Article
- Conserved assembly architecture of the essential herpesvirus packaging accessory factor.bioRxiv : the preprint server for biology · 2026Article
- Nucleus softens during herpesvirus infection.PLoS pathogens · 2026Article
- ER protein CLCC1 promotes nuclear envelope fusion in herpesviral and host processes.Nature communications · 2025Article
- ASFV pE146L-induced ER remodeling is essential for viral replication.Journal of virology · 2025Article
- ESCRT-III is recruited by human herpesvirus 6A nuclear egress complex to promote nuclear egress of the nucleocapsid.Journal of virology · 2025Article
- The loss of both pUL16 and pUL21 in HSV-1-infected cells alters capsid-tegument composition, nuclear membrane architecture, cytoplasmic maturation and cell-to-cell spread.The Journal of general virology · 2025Article
- The loss of both pUL16 and pUL21 in HSV-1 infected cells abolishes cytoplasmic envelopment.bioRxiv : the preprint server for biology · 2024Article
- The TET3 inflammasome senses unique long HSV-1 proteins for virus particle budding from the nucleus.Cellular & molecular immunology · 2024Article
- Current Insights into the Maturation of Epstein-Barr Virus Particles.Microorganisms · 2024Review
- 'Getting Better'-Is It a Feasible Strategy of Broad Pan-Antiherpesviral Drug Targeting by Using the Nuclear Egress-Directed Mechanism?International journal of molecular sciences · 2024Review
- The incredible bulk: Human cytomegalovirus tegument architectures uncovered by AI-empowered cryo-EM.Science advances · 2024Article
- Individual herpes simplex virus 1 (HSV-1) particles exit by exocytosis and accumulate at preferential egress sites.Journal of virology · 2024Article
- The universal suppressor mutation restores membrane budding defects in the HSV-1 nuclear egress complex by stabilizing the oligomeric lattice.PLoS pathogens · 2024Article
- A small molecule exerts selective antiviral activity by targeting the human cytomegalovirus nuclear egress complex.PLoS pathogens · 2023Article
- Human herpesvirus 6A nuclear matrix protein U37 interacts with heat shock transcription factor 1 and activates the heat shock response.Journal of virology · 2023Article
- HSV-1 exploits host heterochromatin for nuclear egress.The Journal of cell biology · 2023Article
- LIVE-CELL FLUORESCENCE MICROSCOPY OF HSV-1 CELLULAR EGRESS BY EXOCYTOSIS.bioRxiv : the preprint server for biology · 2023Article
- Article
46 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors.
Funding
Abstract
The nuclear egress complex (NEC) of herpesviruses such as HSV-1 is essential for the exit of nascent capsids from the cell nucleus. The NEC drives nuclear envelope vesiculation in cells, but the precise budding mechanism and the potential involvement of cellular proteins are unclear. Here we report that HSV-1 NEC alone is sufficient for membrane budding in vitro and thus represents a complete membrane deformation and scission machinery. It forms ordered coats on the inner surface of the budded vesicles, suggesting that it mediates scission by scaffolding the membrane bud and constricting the neck to the point of scission. The inward topology of NEC-mediated budding in vitro resembles capsid budding into the inner nuclear membrane during HSV-1 infection and nuclear envelope vesiculation in NEC-transfected cells. We propose that the NEC functions as minimal virus-encoded membrane-budding machinery during nuclear egress and does not require additional cellular factors.
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