| Affiliations | Department of Health Sciences and Technology, GAIHST, Gachon University, Incheon, Republic of Korea; Department of Genome Medicine and Science, College of Medicine, Gachon University, Incheon, Republic of Korea; New Drug Development Center, Osong Medical Innovation Foundation, Cheongju-si, Republic of Korea; Department of Pharmaceutical Engineering, Sangji University, Wonju, Republic of Korea; Immunitrack, Copenhagen, Denmark; National Center for Bioinformatics, Quaid-i-Azam University, Islamabad, Pakistan; School of Biopharmaceutical and Medical Sciences, Sungshin Women's University, Seoul, Republic of Korea. | |
| Abstract | Human leukocyte antigen (HLA) class I has more than 18,000 alleles, each of which binds to a set of unique peptides from the cellular degradome. Deciphering the interaction between antigenic peptides and HLA proteins is crucial for understanding immune responses in autoimmune diseases and cancer. In this study, we aimed to characterize the peptidome that binds to HLA-A*33:03, which is one of the most prevalent HLA-A alleles in the Northeast Asian population, but poorly studied. For this purpose, we analyzed the HLA-A*33:03 monoallelic B cell line using immunoprecipitation of HLA-A and peptide complexes, followed by liquid chromatography-tandem mass spectrometry (LC-MS/MS). In this study, we identified 5731 unique peptides that were associated with HLA A*33:03, and experimentally validated the affinity of 40 peptides for HLA-A*33:03 and their stability in HLA A*33:03-peptides complexes. To our knowledge, this study represents the largest dataset of peptides associated with HLA-A*33:03. Also, this is the first study in which HLA A*33:03-associated peptides were experimentally validated. | |