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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Vydané v:	Vaccine Ročník 38; číslo 38; s. 6019 - 6026
Hlavní autori:	Liekniņa, Ilva, Černova, Darja, Rūmnieks, Jānis, Tārs, Kaspars
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	Netherlands Elsevier Ltd 27.08.2020 Elsevier Limited Elsevier
Predmet:	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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Abstract	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.
AbstractList	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. 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. AbstractVirus-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. 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.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.
Author	Tārs, Kaspars Liekniņa, Ilva Černova, Darja Rūmnieks, Jānis
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Keywords	ssRNA bacteriophages Virus-like particles VLP vaccines
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Snippet	Virus-like particles (VLPs) can be used as efficient carriers of various antigens and therefore serve as attractive tools in vaccine development. Although VLPs... AbstractVirus-like particles (VLPs) can be used as efficient carriers of various antigens and therefore serve as attractive tools in vaccine development....
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SubjectTerms	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
Title	Novel ssRNA phage VLP platform for displaying foreign epitopes by genetic fusion
URI	https://www.clinicalkey.com/#!/content/1-s2.0-S0264410X20309166 https://www.clinicalkey.es/playcontent/1-s2.0-S0264410X20309166 https://dx.doi.org/10.1016/j.vaccine.2020.07.016 https://www.ncbi.nlm.nih.gov/pubmed/32713683 https://www.proquest.com/docview/2432846410 https://www.proquest.com/docview/2427526076 https://www.proquest.com/docview/2552041634 https://www.osti.gov/biblio/1691804
Volume	38
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