| http://purl.uniprot.org/citations/21992180 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21992180 | http://www.w3.org/2000/01/rdf-schema#comment | "BackgroundHeat shock protein 70 (HSP70) has gained major attention as an adjuvant capable of inducing antigen-specific CD8(+) and CD4(+) T-cell responses. The ability of HSP70/peptide complexes to elicit cytotoxic T-cell (CTL) responses by cross-presentation of exogenous antigens via HLA class I molecules is of central interest in immunotherapy. We examined the role of HSP70/CMVpp65(495-503)-peptide complex (HSP70/CMV-PC) in HLA class I-restricted cross-presentation for ex vivo expansion of CMV-specific CTLs.MethodsCMV-specific T cells generated from PBMCs of HLA-A*02:01/CMV-seropositive donors were stimulated for 21 days with HSP70/CMV-PC and analyzed in functional assays. As a control PBMCs were cultured in the presence of CMVpp65(495-503) peptide or HSP70. Increase of CMV-specific CTLs was visualized by pentameric HLA-A*02:01/CMVpp65(495-503) complex.ResultsAbout 90% of HSP70/CMV-PC generated T cells were CMV-specific and exhibited significantly higher IFN-γ secretion, cytotoxic activity, and an increased heme oxygenase 1 (HO-1) gene expression as compared to about 69% of those stimulated with CMVpp65(495-503) peptide. We decided to classify the HLA-A*02:01/CMV-seropositive donors as weak, medium, and strong responder according to the frequency of generated A2/CMV-pentamer-positive CD8(+) T cells. HSP70/CMV-PC significantly induces strong antiviral T-cell responses especially in those donors with low memory precursor frequencies. Blockage of CD91 with α2-macroglobulin markedly reduced proliferation of antiviral T cells suggesting a major role of this receptor in the uptake of HSP70/CMV-PC.ConclusionThis study clearly demonstrates that HSP70/CMV-PC is a potent mediator to induce stronger T-cell responses compared to antiviral peptides. This simple and efficient technique may help to generate significant quantities of antiviral CTLs by cross-presentation. Thus, we propose HSP70 for chaperoning peptides to reach an efficient level of cross-presentation. HSP70/peptide complexes may be particularly useful to generate stronger T-cell responses in cases of low precursor frequencies and may help to improve the efficiency of antigen-specific T-cell therapy for minor antigens."xsd:string |
| http://purl.uniprot.org/citations/21992180 | http://purl.org/dc/terms/identifier | "doi:10.1186/1479-5876-9-175"xsd:string |
| http://purl.uniprot.org/citations/21992180 | http://purl.uniprot.org/core/author | "Blasczyk R."xsd:string |
| http://purl.uniprot.org/citations/21992180 | http://purl.uniprot.org/core/author | "Eiz-Vesper B."xsd:string |
| http://purl.uniprot.org/citations/21992180 | http://purl.uniprot.org/core/author | "Tischer S."xsd:string |
| http://purl.uniprot.org/citations/21992180 | http://purl.uniprot.org/core/author | "Immenschuh S."xsd:string |
| http://purl.uniprot.org/citations/21992180 | http://purl.uniprot.org/core/author | "Oelke M."xsd:string |
| http://purl.uniprot.org/citations/21992180 | http://purl.uniprot.org/core/author | "Basila M."xsd:string |
| http://purl.uniprot.org/citations/21992180 | http://purl.uniprot.org/core/author | "Maecker-Kolhoff B."xsd:string |
| http://purl.uniprot.org/citations/21992180 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21992180 | http://purl.uniprot.org/core/name | "J Transl Med"xsd:string |
| http://purl.uniprot.org/citations/21992180 | http://purl.uniprot.org/core/pages | "175"xsd:string |
| http://purl.uniprot.org/citations/21992180 | http://purl.uniprot.org/core/title | "Heat shock protein 70/peptide complexes: potent mediators for the generation of antiviral T cells particularly with regard to low precursor frequencies."xsd:string |
| http://purl.uniprot.org/citations/21992180 | http://purl.uniprot.org/core/volume | "9"xsd:string |
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