Molecular interaction and enzymatic activity of macrophage migration inhibitory factor with immunorelevant peptides

Ilaria Potolicchio, Laura Santambrogio, Jack L. Strominger

Research output: Contribution to journalArticle

31 Scopus citations

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 allotypes, 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 β1 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.

Original languageEnglish (US)
Pages (from-to)30889-30895
Number of pages7
JournalJournal of Biological Chemistry
Volume278
Issue number33
DOIs
StatePublished - Aug 15 2003

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Molecular interaction and enzymatic activity of macrophage migration inhibitory factor with immunorelevant peptides'. Together they form a unique fingerprint.

  • Cite this