Sani, M.Z. and Bargahi, A. and Momenzadeh, N. and Dehghani, P. and Moghadam, M.V. and Maleki, S.J. and Nabipour, I. and Shirkani, A. and Akhtari, J. and Hesamizadeh, K. and Heidari, S. and Omrani, F. and Akbarzadeh, S. and Mohammadi, M. (2021) Genetically engineered fusion of allergen and viral-like particle induces a more effective allergen-specific immune response than a combination of them. Applied Microbiology and Biotechnology, 105 (1). pp. 77-91.
Full text not available from this repository.Abstract
Abstract: Chimeric virus-like particles (VLPs) were developed as a candidate for allergen-specific immunotherapy. In this study, hepatitis B core antigen (HBcAg) that genetically fused to Chenopodium album polcalcin (Che a 3)�derived peptide was expressed in E. coli BL21, purified, and VLP formation was evaluated using native agarose gel electrophoresis (NAGE) and transmission electron microscopy (TEM). Chimeric HBc VLPs were characterized in terms of their reactivity to IgE, the induction of blocking IgG and allergen-specific IgE, basophil-activating capacity, and Th1-type immune responses. Results from IgE reactivity and basophil activation test showed that chimeric HBc VLPs lack IgE-binding capacity and basophil degranulation activity. Although chimeric HBc VLPs induced the highest level of efficient polcalcin-specific IgG antibody in comparison to those induced by recombinant Che a 3 (rChe a 3) mixed either with HBc VLPs or alum, they triggered the lowest level of polcalcin-specific IgE in mice following immunization. Furthermore, in comparison to the other antigens, chimeric HBc VLPs produced a polcalcin-specific Th1 cell response. Taken together, genetically fusion of allergen derivatives to HBc VLPs, in comparison to a mix of them, may be a more effective way to induce appropriate immune responses in allergen-specific immunotherapy. Key points: � The insertion of allergen-derived peptide into major insertion region (MIR) of hepatitis B virus core (HBc) antigen resulted in nanoparticles displaying allergen-derived peptide upon its expression in prokaryotic host. � The resultant VLPs (chimeric HBc VLPs) did not exhibit IgE reactivity with allergic patients� sera and were not able to degranulate basophils. � Chimeric HBc VLPs dramatically improved protective IgG antibody response compared with those induced by allergen mixed either with HBc VLPs or alum. � Chimeric HBc VLPs induced Th1 responses that were counterparts of Th2 responses (allergic). � Chimeric HBc VLPs increased IgG2a/ IgG1 ratio and the level of IFN-γ compared to those induced by allergen mixed with either HBc VLPs or alum. Figure not available: see fulltext. © 2020, Springer-Verlag GmbH Germany, part of Springer Nature.
| Item Type: | Article |
|---|---|
| Additional Information: | cited By 0 |
| Uncontrolled Keywords: | Antibodies; Chemical activation; Electrophoresis; Escherichia coli; High resolution transmission electron microscopy; Immune system; Mammals; Peptides; Viruses, Agarose gel electrophoresis; Allergic patients; Antibody response; Hepatitis b core antigens; Hepatitis B virus; IgE reactivities; Immune response; Virus-like particles, Allergens, hepatitis B core antigen; immunoglobulin E; immunoglobulin G antibody; immunoglobulin G1; immunoglobulin G2a antibody; recombinant protein; restriction endonuclease, antibody; antigen; genetic engineering; hepatitis; immune response; immune system; induced response; peptide; virus, adult; agar gel electrophoresis; aqueous solution; Article; basophil activation test; basophil degranulation; Chenopodium album; clinical article; comparative study; competitive inhibition; controlled study; cytokine response; enzyme linked immunosorbent assay; female; genetic engineering; human; immune response; male; nucleotide sequence; plasmid; prick test; protein expression; protein purification; respiratory tract allergy; Th1 cell; transmission electron microscopy; virus like agent, Chenopodium album; Escherichia coli; Hepatitis B virus; Prokaryota |
| Subjects: | WD Disorders of Systemic, Metabolic or Environmental Origin, etc. |
| Depositing User: | eprints admin |
| Date Deposited: | 21 Apr 2021 04:30 |
| Last Modified: | 21 Apr 2021 04:30 |
| URI: | http://eprints.iums.ac.ir/id/eprint/33352 |
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