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J. Biol. Chem., Vol. 282, Issue 7, 4479-4484, February 16, 2007

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Flagellin Contamination of Recombinant Heat Shock Protein 70 Is Responsible for Its Activity on T Cells^*

Zhiyong Ye and Yunn-Hwen Gan¹

From the Department of Biochemistry, Immunology Program, Yong Loo Lin School of Medicine, National University of Singapore, Block MD7, #05-10, 8 Medical Drive, Singapore 117597, Singapore

Heat shock proteins (Hsp) 60 and 70 have been intensively studied for their ability to activate innate immunity. Heat shock proteins had been shown to induce the activation of dendritic cells, T cells, and B cells. However, the possible contamination of endotoxin in heat shock protein preparations makes their function as an activator of immune system ambiguous. Here, we examined the ability of bacterial Hsp60 and Hsp70 to activate Jurkat T cells and primary T cells. We found that Burkholderia pseudomallei Hsp70 and Mycobacterium tuberculosis Hsp70 could costimulate Jurkat T cells to make IL-2 and signal through TLR5. This costimulatory activity is not due to endotoxin or contaminants signaling via TLR2 nor TLR4. However, recombinant Hsp70 expressed in Escherichia coli fliC strain completely lost its ability to costimulate T cells. Thus, the activation of T cells by recombinant Hsp70 is ascribed to flagellin contamination.

Received for publication, July 17, 2006 , and in revised form, November 9, 2006.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains a supplemental figure.

¹ To whom correspondence should be addressed. Tel.: 65-6516-3678; Fax: 65-6779-1453; E-mail: bchganyh{at}nus.edu.sg.

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