PMID: 9652824Jul 4, 1998Paper

A peptide-binding assay for the disease-associated HLA-DQ8 molecule

Scandinavian Journal of Immunology
A StraumforsS Buus

Abstract

The study of peptide binding to HLA class II molecules has mostly concentrated on DR molecules. Since many autoimmune diseases show a primary association to particular DQ molecules rather than DR molecules, it is also important to study the peptide-binding properties of DQ molecules. Here we report a biochemical peptide-binding assay for the type I diabetes-associated DQ8, i.e. DQ (alpha1*0301, beta1*0302), molecule. Affinity-purified DQ8 molecules were tested in peptide-binding assays using a radiolabelled influenza haemagglutinin (Ha) peptide encompassing positions 255-271(Y) as an indicator peptide. The Ha 255-271(Y) peptide bound to DQ8 in a pH-dependent fashion showing optimal binding around pH 5. The association kinetics were relatively slow and the resulting complexes were heat labile. The specificity of peptide binding to DQ8 was investigated in competitive inhibition experiments with a panel of 43 peptides of different lengths and sequences. The DQ8 molecules showed a different pattern of peptide binding compared to a previously studied DQ2 molecule. Peptides derived from thyroid peroxidase, HLA-DQ(alpha1*0301), HLA-DQ(alpha1*0302), retinol receptor and p21ras were among the high-affinity binders, whereas peptides deri...Continue Reading

References

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Citations

Aug 3, 2005·The Journal of Clinical Investigation·Anish SuriEmil R Unanue
Sep 3, 2010·The Journal of Immunology : Official Journal of the American Association of Immunologists·John SidneyAlessandro Sette
Oct 23, 2002·The Journal of Immunology : Official Journal of the American Association of Immunologists·John SidneyAlessandro Sette

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