Enhanced immunogenicity of a positively supercharged archaeon thioredoxin scaffold as a cell-penetrating antigen carrier for peptide vaccines.
antigen carrier
epitope display
intracellular antigen delivery
peptide epitope
protein DNA interaction
protein scaffold engineering
protein scaffold vaccine
recombinant vaccine
Journal
Frontiers in immunology
ISSN: 1664-3224
Titre abrégé: Front Immunol
Pays: Switzerland
ID NLM: 101560960
Informations de publication
Date de publication:
2022
2022
Historique:
received:
31
05
2022
accepted:
19
07
2022
entrez:
29
8
2022
pubmed:
30
8
2022
medline:
31
8
2022
Statut:
epublish
Résumé
Polycationic resurfaced proteins hold great promise as cell-penetrating bioreagents but their use as carriers for the intracellular delivery of peptide immuno-epitopes has not thus far been explored. Here, we report on the construction and functional characterization of a positively supercharged derivative of
Identifiants
pubmed: 36032169
doi: 10.3389/fimmu.2022.958123
pmc: PMC9405434
doi:
Substances chimiques
Antigens
0
Cell-Penetrating Peptides
0
Epitopes, B-Lymphocyte
0
Peptides
0
Vaccines, Subunit
0
Thioredoxins
52500-60-4
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
958123Informations de copyright
Copyright © 2022 Cavazzini, Spagnoli, Mariz, Reggiani, Maggi, Franceschi, Donofrio, Müller, Bolchi and Ottonello.
Déclaration de conflit d'intérêts
PSC PfTrx and +21 PfTrx-(HPV16-L2)3x as well as other thioredoxin derivatives are covered by patents US9303082B2 and US10736954B2, in which some of the authors of the present work (AB, GS, MM and SO) appear as co-inventors. The remaining authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest
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