0000000001280636

AUTHOR

Boris Christian Marincek

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Heat shock protein-antigen fusions lose their enhanced immunostimulatory capacity after endotoxin depletion.

2008

Heat shock proteins (HSPs) induce cross-presentation of antigens by dendritic cells (DC) as well as DC maturation. These properties make HSP antigen complexes good candidates to prime CD8 T cell responses against tumor-associated antigens. In this study, we analyzed four different members of the HSP70 family fused to a fragment of ovalbumin (OVA) as a model tumor antigen. E. coli-derived recombinant HSP70-OVA fusion proteins efficiently primed antigen-specific cytotoxic T cells in short-term in vivo immunization assays. Because of concerns that the adjuvant effect of HSPs may be due to endotoxin contamination, we studied this issue in detail. Induction of OVA-specific cytotoxicity was signi…

Cytotoxicity ImmunologicCpG OligodeoxynucleotideOvalbuminRecombinant Fusion ProteinsImmunologyReceptors Antigen T-CellMice TransgenicBiologyCD8-Positive T-LymphocytesLymphocyte ActivationMiceImmune systemCross-PrimingAntigenAdjuvants ImmunologicHeat shock proteinNeoplasmsCytotoxic T cellAnimalsHSP70 Heat-Shock ProteinsAntigensMolecular BiologyTLR9Dendritic CellsMolecular biologyFusion proteinTumor antigenEndotoxinsMice Inbred C57BLOligodeoxyribonucleotidesT-Lymphocytes CytotoxicMolecular immunology
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