ArticleJournal of virology2000
Analysis of capsid formation of human polyomavirus JC (Tokyo-1 strain) by a eukaryotic expression system: splicing of late RNAs, translation and nuclear transport of major capsid protein VP1, and capsid assembly.
Article in Journal of virology, 2000. 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, 51 citations in OpenAlex.
- JC Virus Agnogene Regulates Histone-Modifying Enzymes via PML-NBs: Transcriptomics in VLP-Expressing Cells.Viruses · 2025Article
- Recent advances in discovery and functional analysis of the small proteins and microRNA expressed by polyomaviruses.Virology · 2025Review
- Revisiting JC virus and progressive multifocal leukoencephalopathy.Journal of neurovirology · 2023Review
- Article
- RepA Promotes the Nucleolar Exclusion of the V2 Protein of Mulberry Mosaic Dwarf-Associated Virus.Frontiers in microbiology · 2020Article
- Development of demyelinating lesions in progressive multifocal leukoencephalopathy (PML): Comparison of magnetic resonance images and neuropathology of post-mortem brain.Neuropathology : official journal of the Japanese Society of Neuropathology · 2019Article
- Expression of novel proteins by polyomaviruses and recent advances in the structural and functional features of agnoprotein of JC virus, BK virus, and simian virus 40.Journal of cellular physiology · 2019Review
- Discovery and characterization of novel trans-spliced products of human polyoma JC virus late transcripts from PML patients.Journal of cellular physiology · 2018Article
- COS-7-based model: methodological approach to study John Cunningham virus replication cycle.Virology journal · 2018Article
- Dynamic Virus-Dependent Subnuclear Localization of the Capsid Protein from a Geminivirus.Frontiers in plant science · 2017Article
- JC virus inclusions in progressive multifocal leukoencephalopathy: scaffolding promyelocytic leukemia nuclear bodies grow with cell cycle transition through an S-to-G2-like state in enlarging oligodendrocyte nuclei.Journal of neuropathology and experimental neurology · 2014Article
- Article
- Article
- Virion assembly factories in the nucleus of polyomavirus-infected cells.PLoS pathogens · 2012Article
- Progressive multifocal leukoencephalopathy and promyelocytic leukemia nuclear bodies: a review of clinical, neuropathological, and virological aspects of JC virus-induced demyelinating disease.Acta neuropathologica · 2010Review
- JC virus: an oncogenic virus in animals and humans?Seminars in cancer biology · 2009Review
- JC virus minor capsid proteins Vp2 and Vp3 are essential for virus propagation.Journal of virology · 2006Article
- Major and minor capsid proteins of human polyomavirus JC cooperatively accumulate to nuclear domain 10 for assembly into virions.Journal of virology · 2004Article
- Intracellular approach for blocking JC virus gene expression by using RNA interference during viral infection.Journal of virology · 2004Article
- Inhibition of virus production in JC virus-infected cells by postinfection RNA interference.Journal of virology · 2004Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human polyomavirus JC (JCV) can encode the three capsid proteins VP1, VP2, and VP3, downstream of the agnoprotein in the late region. JCV virions are identified in the nucleus of infected cells. In this study, we have elucidated unique features of JCV capsid formation by using a eukaryotic expression system. Structures of JCV polycistronic late RNAs (M1 to M4 and possibly M5 and M6) generated by alternative splicing were determined. VP1 would be synthesized from M2 RNA, and VP2 and VP3 would be synthesized from M1 RNA. The presence of the open reading frame of the agnoprotein or the leader sequence (nucleotides 275 to 409) can decrease the expression level of VP1. VP1 was efficiently transported to the nucleus in the presence of VP2 and VP3 but distributed both in the cytoplasm and in the nucleus in their absence. Mutation analysis indicated that inefficiency in nuclear transport of VP1 is due to the unique structure in the N-terminal sequence, KRKGERK. Within the nucleus, VP1 was localized discretely and identified as speckles in the presence of VP2 and VP3 but distributed diffusely in their absence. These results suggest that VP1 was efficiently transported to the nucleus and localized in the discrete subnuclear regions, possibly with VP2 and VP3. By electron microscopy, recombinant virus particles were identified in the nucleus, and their intranuclear distribution was consistent with distribution of speckles. This system provides a useful model with which to understand JCV capsid formation and the structures and functions of the JCV capsid proteins.
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