Arne von Bonin

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Peptides bound or linked to heat-shock proteins (HSPs) of microbial or mammalian origin have been shown to elicit potent antigen-specific immunity. Some members of the HSP family, such as hsp60, hsp70, hsp90 and gp96, are able also to stimulate cells of the innate immune system directly and thus, act as 'danger'-signaling molecules. This effect is(More)
The understanding of chemically induced allergic or autoimmune disorders requires a detailed structural analysis of the antigenic determinants produced by chemical modification of cells. Using H-2Kb-restricted, TNP-specific cytotoxic mouse T cells and synthetic, Kb-associating TNP-peptides, we define at least two types of functionally distinguishable TNP(More)
A possible function of eukaryotic heat shock protein 60 (Hsp60) as endogenous danger signal has been controversially discussed in the past. Hsp60 was shown to induce the secretion of proinflammatory cytokines in professional antigen-presenting cells and to enhance the activation of T cells in primary stimulation. However, in vitro activation of macrophages(More)
Stress-induced proteins or heat shock proteins (HSP) of 96 kDa mass (gp96) and 70 kDa mass (HSP70) have been shown previously to elicit specific immunity to tumors from which they are isolated. This immunity is dependent on CD8+ cytotoxic T cells which are readily primed in vivo by immunization with HSP. The immunization capacity of HSP relies on their(More)
The heat shock proteins (HSP) gp96, Hsp70 and Hsp60 activate professional antigen-presenting cells (APC) to secrete proinflammatory cytokines and to express costimulatory molecules. Here, we analyze the impact of Hsp60 as a hypothetical danger signal on the antigen-specific activation of T cells derived from DO11.10 TCR-transgenic mice. The release of(More)
CD83 is a marker molecule for mature dendritic cells (DCs) but is also substantially expressed on activated T cells in humans and mice. Its function is unknown, but CD83 knockout mice show an impaired thymic maturation of CD4-positive cells and soluble CD83 inhibits partially antigen-specific responses in vitro pointing to a role of CD83 in the immune(More)
Heat shock proteins (Hsp) are ubiquitous intracellular proteins that can be released in various forms of cellular stress. Some Hsp, such as Hsp60, have been shown to stimulate directly T cell-mediated immune responses in vitro. Here, it is demonstrated that Hsp60 is released from the kidneys and excreted into the urine of mice with nephrotoxic nephritis(More)
CD26 or dipeptidylpeptidase IV (DPP IV) is a cell surface protease involved in T cell activation. It is a type II transmembrane glycoprotein consisting of a large extracellular part, a single transmembrane region and a short cytoplasmic tail without any common signalling motifs. To eluciate the mechanisms involved in CD26-mediated signalling we have(More)
CD26 is a proteolytic enzyme (dipeptidyl-peptidase IV) with a wide tissue distribution and a unique specificity that was already described 27 years ago. CD26 is expressed on a fraction of resting T cells at low density but is strongly upregulated following T-cell activation. Recent results indicate that CD26 is a multifunctional molecule that may have(More)
Few studies have addressed the consequences of physical interactions between NK and T cells, as well as physical interactions among NK cells themselves. We show in this study that NK cells can enhance T cell activation and proliferation in response to CD3 cross-linking and specific Ag through interactions between 2B4 (CD244) on NK cells and CD48 on T cells.(More)