ArticleBiophysical journal2009
Retroviral assembly and budding occur through an actin-driven mechanism.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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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
60 citing papers in PubMed, 96 citations in OpenAlex.
- Review
- From viral assembly to host interaction: AFM's contributions to virology.Journal of virology · 2025Review
- HIV-1 budding requires cortical actin disassembly by the oxidoreductase MICAL1.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Extracellular vesicle therapy in neurological disorders.Journal of biomedical science · 2024Review
- Emerging roles of cytoskeletal transport and scaffold systems in human viral propagation.Animal cells and systems · 2024Review
- Mesenchymal stem cell-derived exosomes: Shaping the next era of stroke treatment.Neuroprotection (Chichester, England) · 2023Article
- HIV Infection: Shaping the Complex, Dynamic, and Interconnected Network of the Cytoskeleton.International journal of molecular sciences · 2023Review
- Article
- LIM Kinases, LIMK1 and LIMK2, Are Crucial Node Actors of the Cell Fate: Molecular to Pathological Features.Cells · 2023Review
- High-speed AFM reveals the dynamics of virus budding.Biophysical journal · 2022Article
- Analysis of individual HIV-1 budding event using fast AFM reveals a multiplexed role for VPS4.Biophysical journal · 2022Article
- Three-Dimensional Investigations of Virus-Associated Structures in the Nuclei with White Spot Syndrome Virus (WSSV) Infection in Red Swamp Crayfish (Animals : an open access journal from MDPI · 2022Article
- Review
- Embedding of HIV Egress within Cortical F-Actin.Pathogens (Basel, Switzerland) · 2022Article
- A Role for Extracellular Vesicles in SARS-CoV-2 Therapeutics and Prevention.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2021Review
- On the Role of Curved Membrane Nanodomains, and Passive and Active Skeleton Forces in the Determination of Cell Shape and Membrane Budding.International journal of molecular sciences · 2021Article
- How Physical Factors Coordinate Virus Infection: A Perspective From Mechanobiology.Frontiers in bioengineering and biotechnology · 2021Review
- Budding of a Retrovirus: Some Assemblies Required.Viruses · 2020Review
- Single-particle virology.Biophysical reviews · 2020Review
- How HIV-1 Gag Manipulates Its Host Cell Proteins: A Focus on Interactors of the Nucleocapsid Domain.Viruses · 2020Review
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 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The assembly and budding of a new virus is a fundamental step in retroviral replication. Yet, despite substantial progress in the structural and biochemical characterization of retroviral budding, the underlying physical mechanism remains poorly understood, particularly with respect to the mechanism by which the virus overcomes the energy barrier associated with the formation of high membrane curvature during viral budding. Using atomic force, fluorescence, and transmission electron microscopy, we find that both human immunodeficiency virus and Moloney murine leukemia virus remodel the actin cytoskeleton of their host. These actin-filamentous structures assemble simultaneously with or immediately after the beginning of budding, and disappear as soon as the nascent virus is released from the cell membrane. Analysis of sections of cryopreserved virus-infected cells by transmission electron microscopy reveals similar actin filament structures emerging from every nascent virus. Substitution of the nucleocapsid domain implicated in actin binding by a leucine-zipper domain results in the budding of virus-like particles without remodeling of the cell's cytoskeleton. Notably, viruses carrying the modified nucleocapsid domains bud more slowly by an order of magnitude compared to the wild-type. The results of this study show that retroviruses utilize the cell cytoskeleton to expedite their assembly and budding.
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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.