ArticleProceedings of the National Academy of Sciences of the United States of America1999
Native display of complete foreign protein domains on the surface of hepatitis B virus capsids.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.
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Who cites it
98 citing papers in PubMed, 251 citations in OpenAlex.
- Review
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- [Platform technologies in vaccine development].Bundesgesundheitsblatt, Gesundheitsforschung, Gesundheitsschutz · 2025Review
- The HBV large envelope protein initiates virion assembly by recruiting capsids at membrane rich domains related to late endosome.Cellular and molecular life sciences : CMLS · 2025Article
- Herpes simplex virus assembly and spread in murine skin after infection from the outside.Journal of virology · 2025Article
- Plant-Produced Chimeric Hepatitis E Virus-like Particles as Carriers for Antigen Presentation.Viruses · 2024Article
- Engineering Hepatitis B Virus (HBV) Protein Particles for Therapeutic Delivery.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Cryo-EM structure determination of small therapeutic protein targets at 3 Å-resolution using a rigid imaging scaffold.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
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- GE11-antigen-loaded hepatitis B virus core antigen virus-like particles efficiently bind to TNBC tumor.Frontiers in oncology · 2023Article
- Flagellin/Virus-like Particle Hybrid Platform with High Immunogenicity, Safety, and Versatility for Vaccine Development.ACS applied materials & interfaces · 2022Article
- Structural conservation among variants of the SARS-CoV-2 spike postfusion bundle.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
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- Studies on HBcAg-rBlo t 5-21 Fusion Protein Vaccine That AlleviatesJournal of inflammation research · 2022Article
- The Hepatitis B Virus Nucleocapsid-Dynamic Compartment for Infectious Virus Production and New Antiviral Target.Biomedicines · 2021Review
- Generation of ordered protein assemblies using rigid three-body fusion.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Generation of Antibodies against Foot-and-Mouth-Disease Virus Capsid Protein VP4 Using Hepatitis B Core VLPs as a Scaffold.Life (Basel, Switzerland) · 2021Article
- Asymmetrizing an icosahedral virus capsid by hierarchical assembly of subunits with designed asymmetry.Nature communications · 2021Article
- Covalent protein display on Hepatitis B core-like particles in plants through the in vivo use of the SpyTag/SpyCatcher system.Scientific reports · 2020Article
38 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nucleocapsid of hepatitis B virus (HBV), or HBcAg, is a highly symmetric structure formed by multiple dimers of a single core protein that contains potent T helper epitopes in its 183-aa sequence. Both factors make HBcAg an unusually strong immunogen and an attractive candidate as a carrier for foreign epitopes. The immunodominant c/e1 epitope on the capsid has been suggested as a superior location to convey high immunogenicity to a heterologous sequence. Because of its central position, however, any c/e1 insert disrupts the core protein's primary sequence; hence, only peptides, or rather small protein fragments seemed to be compatible with particle formation. According to recent structural data, the epitope is located at the tips of prominent surface spikes formed by the very stable dimer interfaces. We therefore reasoned that much larger inserts might be tolerated, provided the individual parts of a corresponding fusion protein could fold independently. Using the green fluorescent protein (GFP) as a model insert, we show that the chimeric protein efficiently forms fluorescent particles; hence, all of its structurally important parts must be properly folded. We also demonstrate that the GFP domains are surface-exposed and that the chimeric particles elicit a potent humoral response against native GFP. Hence, proteins of at least up to 238 aa can be natively displayed on the surface of HBV core particles. Such chimeras may not only be useful as vaccines but may also open the way for high resolution structural analyses of nonassembling proteins by electron microscopy.
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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.