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Antigenic Peptide-Thioredoxin Fusion Chimeras for In Vitro Stimulus of CD4+ TCR+ Jurkat T Cellsстатья
Дата последнего поиска статьи во внешних источниках: 5 июня 2024 г.
- Авторы: Ishina I.A., Zakharova M.Y., Kurbatskaia I.N., Mamedov A.E., Belogurov A.A., Rubtsov Yu P., Gabibov A.G.
- Журнал: Doklady Biochemistry and Biophysics
- Том: 516
- Номер: 1
- Год издания: 2024
- Издательство: M A I K Nauka - Interperiodica
- Местоположение издательства: Russian Federation
- Первая страница: 53
- Последняя страница: 57
- DOI: 10.1134/S1607672924600210
- Аннотация: Study of CD4+ T cell response and T cell receptor (TCR) specificity is crucial for understanding etiology of immune-mediated diseases and developing targeted therapies. However, solubility, accessibility, and stability of synthetic antigenic peptides used in T cell assays may be a critical point in such studies. Here we present a T cell activation reporter system using recombinant proteins containing antigenic epitopes fused with bacterial thioredoxin (trx-peptides) and obtained by bacterial expression. We report that co-incubation of CD4+ HA1.7 TCR+ reporter Jurkat 76 TRP cells with CD80+ HLA-DRB1*01:01+ HeLa cells or CD4+ Ob.1A12 TCR+ Jurkat 76 TRP with CD80+ HLA-DRB1*15:01+ HeLa cells resulted in activation of reporter Jurkat 76 TPR after addition of recombinant trx-peptide fusion proteins, containing TCR-specific epitopes. Trx-peptides were comparable with corresponding synthetic peptides in their capacity to activate Jurkat 76 TPR. These data demonstrate that thioredoxin as a carrier protein (trx) for antigenic peptides exhibits minimal interference with recognition of MHC-specific peptides by TCRs and consequent T cell activation. Our findings highlight potential feasibility of trx-peptides as a reagent for assessing the immunogenicity of antigenic fragments.
- Добавил в систему: Агапкина Юлия Юрьевна