Article: article from journal or magazin.
Molecular interaction and enzymatic activity of macrophage migration inhibitory factor with immunorelevant peptides.
Journal of Biological Chemistry
Publication types: Journal Article
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 beta1 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.
Antigen Presentation/immunology, Disulfides/metabolism, Enzyme-Linked Immunosorbent Assay, Hepatitis B Surface Antigens/metabolism, Histocompatibility Antigens Class II/immunology, Histocompatibility Antigens Class II/metabolism, Humans, Insulin/metabolism, Macrophage Migration-Inhibitory Factors/immunology, Macrophage Migration-Inhibitory Factors/metabolism, Oxidoreductases/metabolism, Peptide Fragments/metabolism, Protein Binding/immunology, Substrate Specificity
Web of science
Last modification date