ArticleJournal of virology1999
Nuclear transport of the major capsid protein is essential for adeno-associated virus capsid formation.
Article in Journal of virology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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
31 citing papers in PubMed, 69 citations in OpenAlex.
- Variation of VP2 stoichiometry and deamidation of VP1 during production and their impacts on the transduction efficiency of AAV vectors.Molecular therapy. Methods & clinical development · 2025Article
- Human bocavirus NP1 antagonizes host type I interferon response through repressing the nuclear transport of STAT1.Virulence · 2025Article
- Adeno-associated virus 9 (AAV9) viral proteins VP1, VP2, and membrane-associated accessory protein (MAAP) differentially influenceJournal of virology · 2024Article
- Probe capsid structure stability and dynamics of adeno-associated virus as an important viral vector for gene therapy by hydrogen-deuterium exchange-mass spectrometry.Protein science : a publication of the Protein Society · 2024Article
- Review
- Nuclear entry and egress of parvoviruses.Molecular microbiology · 2022Review
- Cryo-electron Microscopy of Adeno-associated Virus.Chemical reviews · 2022Review
- Recent Advances in Molecular Biology of Human Bocavirus 1 and Its Applications.Frontiers in microbiology · 2021Review
- Intracellular Localization ofViruses · 2018Article
- Foreword to 'Multiscale structural biology: biophysical principles and mechanisms underlying the action of bio-nanomachines', a special issue in Honour of Fumio Arisaka's 70th birthday.Biophysical reviews · 2018Article
- The role of nuclear localization signal in parvovirus life cycle.Virology journal · 2017Review
- Perspective on Adeno-Associated Virus Capsid Modification for Duchenne Muscular Dystrophy Gene Therapy.Human gene therapy · 2015Review
- Recombinant adeno-associated virus utilizes host cell nuclear import machinery to enter the nucleus.Journal of virology · 2014Article
- DNA virus replication compartments.Journal of virology · 2014Review
- Impact of VP1-specific protein sequence motifs on adeno-associated virus type 2 intracellular trafficking and nuclear entry.Journal of virology · 2012Article
- Intracellular transport of recombinant adeno-associated virus vectors.Gene therapy · 2012Review
- A viral assembly factor promotes AAV2 capsid formation in the nucleolus.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Proteolytic mapping of the adeno-associated virus capsid.Molecular therapy : the journal of the American Society of Gene Therapy · 2006Article
- Adeno-associated virus type 2 capsids with externalized VP1/VP2 trafficking domains are generated prior to passage through the cytoplasm and are maintained until uncoating occurs in the nucleus.Journal of virology · 2006Article
- Separate basic region motifs within the adeno-associated virus capsid proteins are essential for infectivity and assembly.Journal of virology · 2006Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Adeno-associated virus capsids are composed of three proteins, VP1, VP2, and VP3. Although VP1 is necessary for viral infection, it is not essential for capsid formation. The other capsid proteins, VP2 and VP3, are sufficient for capsid formation, but the functional roles of each protein are still not well understood. By analyzing a series of deletion mutants of VP2, we identified a region necessary for nuclear transfer of VP2 and found that the efficiency of nuclear localization of the capsid proteins and the efficiency of virus-like particle (VLP) formation correlated well. To confirm the importance of the nuclear localization of the capsid proteins, we fused the nuclear localization signal of simian virus 40 large T antigen to VP3 protein. We show that this fusion protein could form VLP, indicating that the VP2-specific region located on the N-terminal side of the protein is not structurally required. This finding suggests that VP3 has sufficient information for VLP formation and that VP2 is necessary only for nuclear transfer of the capsid proteins.
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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.