ArticleJournal of virology2002
The NS2 proteins of parvovirus minute virus of mice are required for efficient nuclear egress of progeny virions in mouse cells.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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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.
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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.
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Who cites it
42 citing papers in PubMed, 76 citations in OpenAlex.
- Canine parvovirus infection affects host cell nucleolar organization and ribosome biogenesis.Communications biology · 2026Article
- Conserved Nuclear Localization Signal in NS2 Protein of Bombyx Mori Bidensovirus: A Potential Invertebrate ssDNA Virus Trait.Viruses · 2025Article
- Efficient elimination of MELAS-associated m.3243G mutant mitochondrial DNA by an engineered mitoARCUS nuclease.Nature metabolism · 2023Article
- Genomes of the autonomous parvovirus minute virus of mice induce replication stress through RPA exhaustion.PLoS pathogens · 2023Article
- 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
- Nuclear entry and egress of parvoviruses.Molecular microbiology · 2022Review
- 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
- SYNCRIP facilitates porcine parvovirus viral DNA replication through the alternative splicing of NS1 mRNA to promote NS2 mRNA formation.Veterinary research · 2021Article
- Manipulating and elucidating mitochondrial gene expression with engineered proteins.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020Review
- Review
- Article
- Intracellular Localization ofViruses · 2018Article
- Article
- Experimental mitochondria-targeted DNA methylation identifies GpC methylation, not CpG methylation, as potential regulator of mitochondrial gene expression.Scientific reports · 2017Article
- Late Maturation Steps Preceding Selective Nuclear Export and Egress of Progeny Parvovirus.Journal of virology · 2016Article
- Tumor Selectivity of Oncolytic Parvoviruses: From in vitro and Animal Models to Cancer Patients.Frontiers in bioengineering and biotechnology · 2015Review
- Complementation for an essential ancillary non-structural protein function across parvovirus genera.Virology · 2014Article
- Molecular characterization of the small nonstructural proteins of parvovirus Aleutian mink disease virus (AMDV) during infection.Virology · 2014Article
- The use of mitochondria-targeted endonucleases to manipulate mtDNA.Methods in enzymology · 2014Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The small nonstructural NS2 proteins of parvovirus minute virus of mice (MVMp) were previously shown to interact with the nuclear export receptor Crm1. We report here the analysis of two MVM mutant genomic clones generating NS2 proteins that are unable to interact with Crm1 as a result of amino acid substitutions within their nuclear export signal (NES) sequences. Upon transfection of human and mouse cells, the MVM-NES21 and MVM-NES22 mutant genomic clones were proficient in synthesis of the four virus-encoded proteins. While the MVM-NES22 clone was further able to produce infectious mutant virions, no virus could be recovered from cells transfected with the MVM-NES21 clone. Whereas the defect of MVM-NES21 appeared to be complex, the phenotype of MVM-NES22 could be traced back to a novel distinct NS2 function. Infection of mouse cells with the MVM-NES22 mutant led to stronger nuclear retention not only of the NS2 proteins but also of infectious progeny MVM particles. This nuclear sequestration correlated with a severe delay in the release of mutant virions in the medium and with prolonged survival of the infected cell populations compared with wild-type virus-treated cultures. This defect could explain, at least in part, the small size of the plaques generated by the MVM-NES22 mutant when assayed on mouse indicator cells. Altogether, our data indicate that the interaction of MVMp NS2 proteins with the nuclear export receptor Crm1 plays a critical role at a late stage of the parvovirus life cycle involved in release of progeny viruses.
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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.