An assay for peptide binding to HLA-Cw*0102

The assembly assay for peptide binding to class I major histocompatibility complex (MHC) molecules is based on the ability of peptides to stabilize MH C class I molecules synthesized by transporter associated with antigen proc essing (TAP)-deficient cell. The TAP-deficient cell line T2 has previously been used in the assembly assay to analyze peptide binding to HLA-A*0201 an d -B*5101. In this study, we have extended this technique to assay for pept ides binding to endogenous HLA-Cw*0102 molecules. We have analyzed the pept ide binding of 20 peptides with primary anchor motifs for HLA-Cw*0102. One- third of the peptides analyzed bound with high affinity, half of the peptid es examined did not bind, whereas the remaining peptides displayed intermed iate binding activity. Interest in HLA-C molecules has increased significan tly in recent years, since it has been shown that HLA-C molecules both can present peptides to cytotoxic T lymphocytes (CTL) and in addition are able to inhibit natural killer (NK)-mediated lysis.