biostudies-literatureSidney JNIAID NIH HHSPHS HHS2492-503https://www.ebi.ac.uk/biostudies/studies/S-EPMC2935290biostudies-literatureUnknown184(5)Compared with DR and DQ, knowledge of the binding repertoires and specificities of HLA-DP alleles is somewhat limited. However, a growing body of literature has indicated the importance of DP-restricted responses in the context of cancer, allergy, and infectious disease. In the current study, we developed high-throughput binding assays for the five most common HLA-DPB1 alleles in the general worldwide population. Using these assays on a comprehensive panel of single-substitution analogs and large peptide libraries, we derived novel detailed binding motifs for DPB1*0101 and DPB1*0501. We also derived more detailed quantitative motifs for DPB1*0201, DPB1*0401, and DPB1*0402, which were previously characterized on the basis of sets of eluted ligands and/or limited sets of substituted peptidesJournal of immunology (Baltimore, Md. : 1950)Five HLA-DP molecules frequently expressed in the worldwide human population share a common HLA supertypic binding specificity.PMC2935290N01 AI040023N01-700048CN01AI40024N01AI40023N01-AI-40024HHSH266200400006CHHSN266200400006CNgo SPeters BSette ASteen AMoore CSidney JChung JfalseFive HLA-DP molecules frequently expressed in the worldwide human population share a common HLA supertypic binding specificity.Compared with DR and DQ, knowledge of the binding repertoires and specificities of HLA-DP alleles is somewhat limited. However, a growing body of literature has indicated the importance of DP-restricted responses in the context of cancer, allergy, and infectious disease. In the current study, we developed high-throughput binding assays for the five most common HLA-DPB1 alleles in the general worldwide population. Using these assays on a comprehensive panel of single-substitution analogs and large peptide libraries, we derived novel detailed binding motifs for DPB1*0101 and DPB1*0501. We also derived more detailed quantitative motifs for DPB1*0201, DPB1*0401, and DPB1*0402, which were previously characterized on the basis of sets of eluted ligands and/or limited sets of substituted peptides2010-01-01T00:00:00Z2010 Mar2025-04-05T00:25:36.827Z2019-03-26T23:42:52ZS-EPMC29352902013927910.4049/jimmunol.0903655