Characterization of HLA-A*33:03 epitopes via immunoprecipitation and LC-MS/MS.
Proteomics
; 22(1-2): e2100171, 2022 01.
Article
en En
| MEDLINE
| ID: mdl-34561969
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*3303, 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*3303 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*3303, and experimentally validated the affinity of 40 peptides for HLA-A*3303 and their stability in HLA A*3303-peptides complexes. To our knowledge, this study represents the largest dataset of peptides associated with HLA-A*3303. Also, this is the first study in which HLA A*3303-associated peptides were experimentally validated.
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Texto completo:
1
Base de datos:
MEDLINE
Asunto principal:
Antígenos HLA-A
/
Espectrometría de Masas en Tándem
Idioma:
En
Revista:
Proteomics
Asunto de la revista:
BIOQUIMICA
Año:
2022
Tipo del documento:
Article