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The Journal of Immunology, 2005, 175: 3594-3602.
Copyright © 2005 by The American Association of Immunologists

Heat Shock Protein 60 Activates B Cells via the TLR4-MyD88 Pathway1

Michal Cohen-Sfady*, Gabriel Nussbaum*,{dagger}, Meirav Pevsner-Fischer*, Felix Mor*, Pnina Carmi*, Alexandra Zanin-Zhorov*, Ofer Lider2,* and Irun R. Cohen3,*

* Department of Immunology, Weizmann Institute of Science, Rehovot, Israel; and {dagger} Hebrew University-Hadassah School of Dental Medicine, Jerusalem, Israel

We recently reported that soluble 60-kDa heat shock protein (HSP60) can directly activate T cells via TLR2 signaling to enhance their Th2 response. In this study we investigated whether HSP60 might also activate B cells by an innate signaling pathway. We found that human HSP60 (but not the Escherichia coli GroEL or the Mycobacterial HSP65 molecules) induced naive mouse B cells to proliferate and to secrete IL-10 and IL-6. In addition, the HSP60-treated B cells up-regulated their expression of MHC class II and accessory molecules CD69, CD40, and B7-2. We tested the functional ability of HSP60-treated B cells to activate an allogeneic T cell response and found enhanced secretion of both IL-10 and IFN-{gamma} by the responding T cells. The effects of HSP60 were found to be largely dependent on TLR4 and MyD88 signaling; B cells from TLR4-mutant mice or from MyD88 knockout mice showed decreased responses to HSP60. Care was taken to rule out contamination of the HSP60 with LPS as a causative factor. These findings add B cells to the complex web of interactions by which HSP60 can regulate immune responses.




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