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J. Biol. Chem., Vol. 278, Issue 33, 30889-30895, August 15, 2003

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Molecular Interaction and Enzymatic Activity of Macrophage Migration Inhibitory Factor with Immunorelevant Peptides^*

Ilaria Potolicchio  , Laura Santambrogio  and Jack L. Strominger  ¶

From the Department of Molecular Cell Biology, Harvard University, Cambridge, Massachusetts 02138 and Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Boston, Massachusetts 02115

Disulfide reduction is an important step in antigen processing for HLA class II restricted T cell responses. Migration inhibitory factor (MIF) is a member of the thioredoxin family and has been classically defined as a cytokine. Using enzyme-linked immunosorbent assay and CD analysis, here we describe the binding to MIF of two peptides, hepatitis B surface antigen (HBsAg) and insulin B (InsB) with high affinity for HLA class II allo-types, HLA-DP2 and HLA-DQ8, respectively. At neutral pH, cysteinylated InsB was a substrate for MIF thiol reductase activity, as assessed by mass spectroscopy/electrospray analysis. Finally, a biologically active form of MIF co-immunopurified with mature forms of HLA DP2/15, and a peptide derived from the HLA-DP 1 helix could be used for affinity purification of MIF. The possibility that MIF participates in class II antigen presentation and/or as a chaperone is discussed.

Received for publication, March 20, 2003 , and in revised form, May 7, 2003.

^* This work was supported by National Institutes of Health Grants AI-49524 and CA-47554 (to J. L. S.) and AI-48832 (to L. S.). 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.

^¶ To whom correspondence may be addressed. Tel.: 617-495-2733; Fax: 617-496-8351; E-mail: ipotolic{at}mcb.harvard.edu or jlstrom{at}fas.harvard.edu.

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