ArticleBiotechnology and bioengineering2022
Differential N- and O-glycosylation signatures of HIV-1 Gag virus-like particles and coproduced extracellular vesicles.
Article in Biotechnology and bioengineering, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Development of a scalable production bioprocess for HIV-1 virus-like particles coupling continuous VLP harvesting with end-to-end downstream processing.Scientific reports · 2026Article
- Glycosylated Foot-And-Mouth Disease Virus-Like Particles Produced in Pichia Pastoris Enhance Stability and Immunogenicity.Microbial biotechnology · 2025Article
- Impact of specific productivity and operation mode upon the biophysical properties of HIV-1 Gag-based virus-like particles.Applied microbiology and biotechnology · 2025Article
- Gag HIV-1 Virus-like Particles and Extracellular Vesicles Functionalization with Spike Epitopes of SARS-CoV-2 Using a Copper-Free Click Chemistry Approach.Bioconjugate chemistry · 2025Article
- Compositional data analysis enables statistical rigor in comparative glycomics.Nature communications · 2025Article
- O-glycosylation in viruses: A sweet tango.mLife · 2024Review
- Construction of a novel kinetic model for the production process of a CVA6 VLP vaccine in CHO cells.Cytotechnology · 2024Article
- Differential N- and O-glycosylation signatures of HIV-1 Gag virus-like particles and coproduced extracellular vesicles.Biotechnology and bioengineering · 2022Article
- How promising are HIV-1-based virus-like particles for medical applications.Frontiers in cellular and infection microbiology · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human immunodeficiency virus 1 (HIV-1) virus-like particles (VLPs) are nanostructures derived from the self-assembly and cell budding of Gag polyprotein. Mimicking the native structure of the virus and being noninfectious, they represent promising candidates for the development of new vaccines as they elicit a strong immune response. In addition to this, the bounding membrane can be functionalized with exogenous antigens to target different diseases. Protein glycosylation depends strictly on the production platform and expression system used and the displayed glycosylation patterns may influence downstream processing as well as the immune response. One of the main challenges for the development of Gag VLP production bioprocess is the separation of VLPs and coproduced extracellular vesicles (EVs). In this study, porous graphitized carbon separation method coupled with mass spectrometry was used to characterize the N- and O- glycosylation profiles of Gag VLPs produced in HEK293 cells. We identified differential glycan signatures between VLPs and EVs that could pave the way for further separation and purification strategies to optimize downstream processing and move forward in VLP-based vaccine production technology.
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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.