Molecular interaction and enzymatic activity of macrophage migration inhibitory factor with immunorelevant peptides.
Details
Serval ID
serval:BIB_187DEF0175E6
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Molecular interaction and enzymatic activity of macrophage migration inhibitory factor with immunorelevant peptides.
Journal
Journal of Biological Chemistry
ISSN
0021-9258
Publication state
Published
Issued date
08/2003
Peer-reviewed
Oui
Volume
278
Number
33
Pages
30889-30895
Language
english
Notes
Publication types: Journal Article
Abstract
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.
Keywords
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
Pubmed
Web of science
Open Access
Yes
Create date
25/01/2008 15:16
Last modification date
20/08/2019 12:48