Comparison of Bacterial Expression Systems Based on Potato Virus Y-like Particles for Vaccine Generation

Plant-based virus-like particle (VLP) vaccines have been studied for years, demonstrating their potential as antigen-presenting platforms. In this paper, we describe the development of, and compare between, simple Escherichia coli-based antigen display platforms for the generation of potato virus Y...

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Vydáno v:Vaccines (Basel) Ročník 10; číslo 4; s. 485
Hlavní autoři: Ogrina, Anete, Skrastina, Dace, Balke, Ina, Kalnciema, Ieva, Jansons, Juris, Bachmann, Martin F., Zeltins, Andris
Médium: Journal Article
Jazyk:angličtina
Vydáno: Switzerland MDPI AG 22.03.2022
MDPI
Témata:
Allergens
Allergies
Animal models
Antibodies
Antigen presentation
Antigens
Avidity
Capsids
Cats
Cell culture
Cloning
Coat protein
Conjugation
E coli
Enzymes
Escherichia coli
expression
Fel d 1
Fel d 1 antigen
Genes
Immunization
Immunoglobulin G
Immunology
Mammals
Monoclonal antibodies
Mutagenesis
Pets
Plant viruses
potato virus Y
Potatoes
Proteins
Systems analysis
Vaccines
Viral infections
Virus-like particles
Viruses
United States > US
virus-like particles
expression
potato virus Y
Fel d 1
E. coli
ISSN:2076-393X, 2076-393X
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Shrnutí:Plant-based virus-like particle (VLP) vaccines have been studied for years, demonstrating their potential as antigen-presenting platforms. In this paper, we describe the development of, and compare between, simple Escherichia coli-based antigen display platforms for the generation of potato virus Y (PVY) VLP-derived vaccines, thus allowing the production of vaccines from a single bacterial cell culture. We constructed four systems with the major cat allergen Fel d 1; namely, direct fusion with plant virus PVY coat protein (CP), mosaic PVY VLPs, and two coexpression variants of conjugates (SpyTag/SpyCatcher) allowing coexpression and conjugation directly in E. coli cells. For control experiments, we included PVY VLPs chemically coupled with Fel d 1. All constructed PVY–Fel d 1 variants were well expressed and soluble, formed PVY-like filamentous particles, and were recognized by monoclonal Fel d 1 antibodies. Our results indicate that all vaccine variants induced high titers of anti-Fel d 1 antibodies in murine models. Mice that were immunized with the chemically coupled Fel d 1 antigen exhibited the highest antibody titers and antibody–antigen interaction specificity, as detected by binding avidity and recognition of native Fel d 1. IgG1 subclass antibodies were found to be the dominant IgG class against PVY–Fel d 1. PVY CP-derived VLPs represent an efficient platform for the comparison of various antigen presentation systems to help evaluate different vaccine designs.
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ISSN:2076-393X
2076-393X
DOI:10.3390/vaccines10040485