Novel ssRNA phage VLP platform for displaying foreign epitopes by genetic fusion

Virus-like particles (VLPs) can be used as efficient carriers of various antigens and therefore serve as attractive tools in vaccine development. Although VLPs of different viruses can be used, VLPs of ssRNA phages have convincing advantages due to their unique properties, including efficient protei...

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Published in:Vaccine Vol. 38; no. 38; pp. 6019 - 6026
Main Authors: Liekniņa, Ilva, Černova, Darja, Rūmnieks, Jānis, Tārs, Kaspars
Format: Journal Article
Language:English
Published: Netherlands Elsevier Ltd 27.08.2020
Elsevier Limited
Elsevier
Subjects:
Allergy and Immunology
Antibodies
Antigens
Bacteriophages
Coat protein
coat proteins
Coating
Disease
Epitopes
Epitopes - genetics
Genetic engineering
Genomes
Humans
Influenza
Influenza Vaccines
Influenza, Human
Leviviridae
Mutation
peptides
Phages
Plasmids
Production costs
protein synthesis
Proteins
ssRNA bacteriophages
Vaccine development
Vaccines
Vaccines, Virus-Like Particle - genetics
Virus-like particles
Viruses
VLP vaccines
Yeast
yeasts
ssRNA bacteriophages
Virus-like particles
VLP vaccines
ISSN:0264-410X, 1873-2518, 1873-2518
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Summary:Virus-like particles (VLPs) can be used as efficient carriers of various antigens and therefore serve as attractive tools in vaccine development. Although VLPs of different viruses can be used, VLPs of ssRNA phages have convincing advantages due to their unique properties, including efficient protein production in bacterial and yeast expression systems, low production cost and easy and fast purification. Currently, the range of ssRNA phage VLPs is limited. In particular, this is true for VLPs that tolerate insertions at the N- and C-termini of the coat protein. It is therefore necessary to find new alternatives within the known ssRNA phage VLP range. From previous studies, we found approximately 80 new VLPs forming ssRNA phage coat proteins. In the current study, we attached a model peptide to the N- and C-termini of coat proteins. As a model peptide, we used a triple repeat of 23 N-terminal residues of the ectodomain of the influenza M2 protein, used previously in the development of the flu vaccine. Examining 43 novel phage coat proteins for the ability to form chimeric VLPs, we found ten new promising candidates for further vaccine design, five of which were tolerant to insertions at both the N- and C-termini. Furthermore, we demonstrate that most of the chimeric VLPs have good antigenic properties as judged from their reactivity with anti-M2 antibodies.
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USDOE Office of Electricity (OE), Advanced Grid Research & Development. Power Systems Engineering Research
1/16/A/104
ISSN:0264-410X
1873-2518
1873-2518
DOI:10.1016/j.vaccine.2020.07.016