Cell
ArticleThe human class II MHC protein HLA-DR1 assembles as empty αβ heterodimers in the absence of antigenic peptide
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Partnering for the major histocompatibility complex class II and antigenic determinant requires flexibility and chaperons
2021, Current Opinion in ImmunologyMHC-I peptide binding activity assessed by exchange after cleavage of peptide covalently linked to β2-microglobulin
2019, Analytical BiochemistryCitation Excerpt :Dipeptides have been identified for some MHC-I proteins that could serve this purpose [27], but a “conditional ligand” strategy has proven more useful, wherein MHC-I complexes are folded with full-length peptides carrying photocleavable [28] or chemically-labile [29] amino acid residues that upon cleavage produce easily-exchangeable peptide fragments. Similar assays have been developed for evaluating affinities of MHC-II epitopes [11,30–34], facilitated in many cases by the increased stability of peptide-free MHC-II relative to MHC-I [35], and by the availability of recombinant MHC-II proteins expressed in E. coli or insect cells with empty peptide-binding sites or carrying only weakly-associating peptides [35–38]. Here, we describe a novel technique to measure peptide affinities, which incorporates a different mode of peptide exchange based on a previously described covalent peptide approach.
HLA-do modulates the diversity of the MHC-ii self-peptidome
2019, Molecular and Cellular ProteomicsCitation Excerpt :Summed areas were then compared with the corresponding heavy peptide areas to determine absolute amount of peptide. Soluble extracellular domains of recombinant HLA-DR1 (DR1) (DRA*0101/DRB1*0101) and DM (DMA*0101/DMB*0101) for binding affinity and DM sensitivity measurements were expressed in Drosophila S2 cells and purified by immunoaffinity chromatography followed by Superdex200 (GE Healthcare, Chicago, IL) size exclusion chromatography as previously described (18, 53). For three abundant self-peptides, DM sensitivity has been previously characterized: CLIP, the invariant chain chaperone fragment efficiently removed by DM (18, 54), DRα52–68, the human ortholog of the YAe epitope (55) known to be highly sensitive to DM exchange (56), and the transplantation alloepitope A2104–117 (39) previously demonstrated to be highly resistant to DM-mediated exchange (38).