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. 2022 Jan;22(1-2):e2100171.
doi: 10.1002/pmic.202100171. Epub 2021 Oct 5.

Characterization of HLA-A*33:03 epitopes via immunoprecipitation and LC-MS/MS

Amir Khan  1   2 , Ji-Yon Shin  1 , Min Kyung So  3 , Jung-Hyun Na  4 , Sune Justesen  5 , Adnan Ahmad Ansari  6 , Byoung Joon Ko  7 , Sung-Min Ahn  1   2
Affiliations

Characterization of HLA-A*33:03 epitopes via immunoprecipitation and LC-MS/MS

Amir Khan et al. Proteomics. 2022 Jan.

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.

Keywords: HLA-A*33:03; cancer vaccine; epitope; human leukocyte antigen; mass spectrometry.

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References

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