ArticleJournal of virology2004
Nuclear export of the nonenveloped parvovirus virion is directed by an unordered protein signal exposed on the capsid surface.
Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
What it found
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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
40 citing papers in PubMed, 73 citations in OpenAlex.
- The role of post-translational modifications in parvovirus life cycle.Frontiers in veterinary science · 2025Review
- Tracking of Human Parvovirus B19 Virus-Like Particles Using Short Peptide Tags Reveals a Membrane-Associated Extracellular Release of These Particles.Journal of virology · 2023Article
- Dextran sulfate fromFrontiers in microbiology · 2023Article
- Nuclear entry and egress of parvoviruses.Molecular microbiology · 2022Review
- Parvovirus nonstructural protein 2 interacts with chromatin-regulating cellular proteins.PLoS pathogens · 2022Article
- Particle-based analysis elucidates the real retention capacities of virus filters and enables optimal virus clearance study design with evaluation systems of diverse virological characteristics.Biotechnology progress · 2022Article
- G2/M checkpoint regulation and apoptosis facilitate the nuclear egress of parvoviral capsids.Frontiers in cell and developmental biology · 2022Article
- Concepts to Reveal Parvovirus-Nucleus Interactions.Viruses · 2021Review
- Cellular p32 Is a Critical Regulator of Porcine Circovirus Type 2 Nuclear Egress.Journal of virology · 2019Article
- Intracellular Localization ofViruses · 2018Article
- Systematic analysis of biological roles of charged amino acid residues located throughout the structured inner wall of a virus capsid.Scientific reports · 2018Article
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- Protoparvovirus Cell Entry.Viruses · 2017Review
- Structural basis for biologically relevant mechanical stiffening of a virus capsid by cavity-creating or spacefilling mutations.Scientific reports · 2017Article
- Structural Analysis of a Temperature-Induced Transition in a Viral Capsid Probed by HDX-MS.Biophysical journal · 2017Article
- Parvovirus Capsid Structures Required for Infection: Mutations Controlling Receptor Recognition and Protease Cleavages.Journal of virology · 2017Article
- Late Maturation Steps Preceding Selective Nuclear Export and Egress of Progeny Parvovirus.Journal of virology · 2016Article
- Reorganization of Nuclear Pore Complexes and the Lamina in Late-Stage Parvovirus Infection.Journal of virology · 2015Article
- Role of capsid proteins in parvoviruses infection.Virology journal · 2015Review
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 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It is uncertain whether nonenveloped karyophilic virus particles may actively traffic from the nucleus outward. The unordered amino-terminal domain of the VP2 major structural protein (2Nt) of the icosahedral parvovirus minute virus of mice (MVM) is internal in empty capsids, but it is exposed outside of the shell through the fivefold axis of symmetry in virions with an encapsidated single-stranded DNA genome, as well as in empty capsids subjected to a heat-induced structural transition. In productive infections of transformed and normal fibroblasts, mature MVM virions were found to efficiently exit from the nucleus prior to cell lysis, in contrast to the extended nuclear accumulation of empty capsids. Newly formed mutant viruses lacking the three phosphorylated serine residues of 2Nt were hampered in their exit from the human transformed NB324K nucleus, in correspondence with the capacity of 2Nt to drive microinjected phosphorylated heated capsids out of the nucleus. However, in normal mouse A9 fibroblasts, in which the MVM capsid was phosphorylated at similar sites but with a much lower rate, the nuclear exit of virions and microinjected capsids harboring exposed 2Nt required the infection process and was highly sensitive to inhibition of the exportin CRM1 in the absence of a demonstrable interaction. Thus, the MVM virion exits the nucleus by accessing nonconventional export pathways relying on cell physiology that can be intensified by infection but in which the exposure of 2Nt remains essential for transport. The flexible 2Nt nuclear transport signal may illustrate a common structural solution used by nonenveloped spherical viruses to propagate in undamaged host tissues.
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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.