Journal
TISSUE ANTIGENS
Volume 59, Issue 4, Pages 251-258Publisher
BLACKWELL MUNKSGAARD
DOI: 10.1034/j.1399-0039.2002.590402.x
Keywords
ELISA; MHC class I; peptide-MHC interaction; W6/32
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Funding
- NIAID NIH HHS [AI49213-02] Funding Source: Medline
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Many different assays for measuring peptide-MHC interactions have been suggested over the years. Yet, there is no generally accepted standard method available. We have recently generated preoxidized recombinant MHC class I molecules (MHC-I) which can be purified to homogeneity under denaturing conditions (i.e., in the absence of any contaminating peptides). Such denatured MHC-I molecules are functional equivalents of empty molecules. When diluted into aqueous buffer containing beta-2 microglobulin (beta(2) m) and the appropriate peptide, they fold rapidly and efficiently in an entirely peptide dependent manner. Here, we exploit the availability of these molecules to generate a quantitative ELISA-based assay capable of measuring the affinity of the interaction between peptide and MHC-I. This assay is simple and sensitive, and one can easily envisage that the necessary reagents, standards and protocols could be made generally available to the scientific community.
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