ArticleProceedings of the National Academy of Sciences of the United States of America2002
HIV type 1 Gag virus-like particle budding from spheroplasts of Saccharomyces cerevisiae.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 74 citations in OpenAlex.
- Yeast vaccine production platform for human and animal infectious diseases.Frontiers in immunology · 2025Review
- Precise Therapy Using the Selective Endogenous Encapsidation for Cellular Delivery Vector System.Pharmaceutics · 2024Review
- Selective extraction of recombinant membrane proteins from Hansenula polymorpha by pulsed electric field and lytic enzyme pretreatment.Microbial cell factories · 2023Article
- Yeast-Based Virus-like Particles as an Emerging Platform for Vaccine Development and Delivery.Vaccines · 2023Review
- Article
- Hepatitis B core-based virus-like particles: A platform for vaccine development in plants.Biotechnology reports (Amsterdam, Netherlands) · 2021Review
- HIV-1 Gag release from yeast reveals ESCRT interaction with the Gag N-terminal protein region.The Journal of biological chemistry · 2020Article
- Different applications of virus-like particles in biology and medicine: Vaccination and delivery systems.Biopolymers · 2016Review
- Current Advances in Virus-Like Particles as a Vaccination Approach against HIV Infection.Vaccines · 2016Review
- Article
- Biological and biochemical characterization of HIV-1 Gag/dgp41 virus-like particles expressed in Nicotiana benthamiana.Plant biotechnology journal · 2013Article
- Trans-packaging of human immunodeficiency virus type 1 genome into Gag virus-like particles in Saccharomyces cerevisiae.Microbial cell factories · 2013Article
- Review
- HIV-1 virus-like particles produced by stably transfected Drosophila S2 cells: a desirable vaccine component.Journal of virology · 2012Article
- ESCRT-independent budding of HIV-1 gag virus-like particles from Saccharomyces cerevisiae spheroplasts.PloS one · 2012Article
- Design and immunogenicity assessment of HIV-1 virus-like particles as a candidate vaccine.Science China. Life sciences · 2011Article
- Novel postentry inhibitor of human immunodeficiency virus type 1 replication screened by yeast membrane-associated two-hybrid system.Antimicrobial agents and chemotherapy · 2011Article
- The cellular factors Vps18 and Mon2 are required for efficient production of infectious HIV-1 particles.Journal of virology · 2011Article
- Effect of mucosal and systemic immunization with virus-like particles of severe acute respiratory syndrome coronavirus in mice.Immunology · 2010Article
- Biological gene delivery vehicles: beyond viral vectors.Molecular therapy : the journal of the American Society of Gene Therapy · 2009Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Expression of retroviral Gag protein in yeast has previously shown Gag targeting to the plasma membrane but little or no production of Gag virus-like particles (VLPs). Here we show that, after removal of the cell wall, the expression of HIV type 1 Gag protein in Saccharomyces cerevisiae spheroplasts allowed simultaneous budding of VLPs from the plasma membrane. Our data show that (i) the VLPs released from yeast spheroplasts were spherical and had morphological features, such as membrane apposed electron-dense layers, characteristic of the immature form of HIV particles; (ii) the VLPs were completely enclosed in the plasma membrane derived from yeast, which is denser than that of higher eukaryotic cells; (iii) the VLP Gag shells remained intact after treatment of nonionic detergent; and (iv) the VLPs were released soon after removal of the cell wall and accumulated up to 300 microg/liter of culture. Our results also show that VLP production was abolished by amino acid substitution of the Gag N-terminal myristoylglycine and impaired when Gag C-terminal deletions were extended beyond the nucleocapsid domain. These results were consistent with those obtained previously in higher eukaryotic expression systems, suggesting that similar Gag domains were used for VLP assembly. We suggest that the system described here offers significant advantages for studying host factors required for VLP budding. The system also may be available for production of vector virus-free VLPs for practical applications such as vaccine development.
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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.