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| Home > Publications database > Enhanced immunogenicity of a positively supercharged archaeon thioredoxin scaffold as a cell-penetrating antigen carrier for peptide vaccines. > print |
| 001 | 181524 | ||
| 005 | 20240229145649.0 | ||
| 024 | 7 | _ | |a 10.3389/fimmu.2022.958123 |2 doi |
| 024 | 7 | _ | |a pmid:36032169 |2 pmid |
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| 037 | _ | _ | |a DKFZ-2022-02059 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 610 |
| 100 | 1 | _ | |a Cavazzini, Davide |b 0 |
| 245 | _ | _ | |a Enhanced immunogenicity of a positively supercharged archaeon thioredoxin scaffold as a cell-penetrating antigen carrier for peptide vaccines. |
| 260 | _ | _ | |a Lausanne |c 2022 |b Frontiers Media |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1661937127_13424 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a 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 Pyrococcus furiosus thioredoxin (PfTrx), a thermally hyperstable protein we have previously validated as a peptide epitope display and immunogenicity enhancing scaffold. Genetic conversion of 13 selected amino acids to lysine residues conferred to PfTrx a net charge of +21 (starting from the -1 charge of the wild-type protein), along with the ability to bind nucleic acids. In its unfused form, +21 PfTrx was readily internalized by HeLa cells and displayed a predominantly cytosolic localization. A different intracellular distribution was observed for a +21 PfTrx-eGFP fusion protein, which although still capable of cell penetration was predominantly localized within endosomes. A mixed cytosolic/endosomal partitioning was observed for a +21 PfTrx derivative harboring three tandemly repeated copies of a previously validated HPV16-L2 (aa 20-38) B-cell epitope grafted to the display site of thioredoxin. Compared to its wild-type counterpart, the positively supercharged antigen induced a faster immune response and displayed an overall superior immunogenicity, including a substantial degree of self-adjuvancy. Altogether, the present data point to +21 PfTrx as a promising novel carrier for intracellular antigen delivery and the construction of potentiated recombinant subunit vaccines. |
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| 588 | _ | _ | |a Dataset connected to CrossRef, PubMed, , Journals: inrepo02.dkfz.de |
| 650 | _ | 7 | |a antigen carrier |2 Other |
| 650 | _ | 7 | |a epitope display |2 Other |
| 650 | _ | 7 | |a intracellular antigen delivery |2 Other |
| 650 | _ | 7 | |a peptide epitope |2 Other |
| 650 | _ | 7 | |a protein DNA interaction |2 Other |
| 650 | _ | 7 | |a protein scaffold engineering |2 Other |
| 650 | _ | 7 | |a protein scaffold vaccine |2 Other |
| 650 | _ | 7 | |a recombinant vaccine |2 Other |
| 700 | 1 | _ | |a Spagnoli, Gloria |b 1 |
| 700 | 1 | _ | |a Mariz, Filipe Colaco |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Reggiani, Filippo |b 3 |
| 700 | 1 | _ | |a Maggi, Stefano |b 4 |
| 700 | 1 | _ | |a Franceschi, Valentina |b 5 |
| 700 | 1 | _ | |a Donofrio, Gaetano |b 6 |
| 700 | 1 | _ | |a Müller, Martin |0 P:(DE-He78)4cbf38280ce272e37f96081b070dd46a |b 7 |u dkfz |
| 700 | 1 | _ | |a Bolchi, Angelo |b 8 |
| 700 | 1 | _ | |a Ottonello, Simone |b 9 |
| 773 | _ | _ | |a 10.3389/fimmu.2022.958123 |g Vol. 13, p. 958123 |0 PERI:(DE-600)2606827-8 |p 958123 |t Frontiers in immunology |v 13 |y 2022 |x 1664-3224 |
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