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 Blood, 26 March 2009, Vol. 113, No. 13, pp. 3008-3016.
Prepublished online as a Blood First Edition Paper on November 18, 2008; DOI 10.1182/blood-2008-06-162727.

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IMMUNOBIOLOGY

Heat shock protein 70 (HSP70) induces cytotoxicity of T-helper cells

Constança Figueiredo1, Miriam Wittmann2, Dong Wang2, Ralf Dressel3, Axel Seltsam1, Rainer Blasczyk1, and Britta Eiz-Vesper1

1 Institute for Transfusion Medicine, Hannover Medical School, Hannover; 2 Department of Immunodermatology and Allergy Research, Hannover Medical School, Hannover; and 3 Department of Cellular and Molecular Immunology, University of Göttingen, Göttingen, Germany

Heat shock protein 70 (HSP70) has gained plenty of attention because of its adjuvant capability to induce CD8+ cytotoxic T lymphocyte and CD4+ T-helper cell responses. We investigated the behavior of T-cell subsets stimulated with endotoxin-free HSP70 with respect to proliferation, cytokine expression, cytotoxicity against allogeneic B-lymphoblastoid cell line and K562 cells, as well as target-independent cytotoxicity. CD4+ cells exhibited a strong increase in proliferation after stimulation with HSP70 (29%). In the presence of targets, a 35-fold up-regulation of granzyme B was observed after stimulation of CD4+ T cells with HSP70 in combination with interleukin-7 (IL-7)/IL-12/IL-15. The target cell-independent secretion of granzyme B by CD4+ cells was greatly augmented after stimulation with HSP70 plus IL-2 or IL-7/IL-12/IL-15. In this study, we showed that HSP70 is capable of inducing a cytotoxic response of T-helper cells in the absence of lipopolysaccharide. The granzyme B secretion and cytolytic activity of T-helper cells are induced in a target-independent way, whereas the cytotoxic activity of CD3+ and CD8+ T cells can be further enhanced in the presence of target cells. Our data provide novel insights into the role of extracellular HSP70 on T-cell immune response concerning the induction of target-independent T-helper cell cytotoxicity.


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