ArticleJournal of proteome research2021
Mild Acid Elution and MHC Immunoaffinity Chromatography Reveal Similar Albeit Not Identical Profiles of the HLA Class I Immunopeptidome.
Article in Journal of proteome research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 53 citations in OpenAlex.
- A Platform for High-throughput and Ultrasensitive Immunopeptidomics.Molecular & cellular proteomics : MCP · 2026Article
- Identification of MHC Ligands Through Allele-Guided Isolation Combined With Machine Learning for Improved MHC Assignment Using ARDisplay-I.Molecular & cellular proteomics : MCP · 2026Article
- Immunopeptidomics of blood coagulation factor IX: a core peptide derived from the protease domain is promiscuously presented on HLA-DR.Research and practice in thrombosis and haemostasis · 2026Article
- Dissection of the T cell infiltrate in mouse pancreatic tumors reveals an extensive and diverse tumor-reactive T cell repertoire.Science advances · 2026Article
- Biomarkers and advances in AML-MRC: from bench to bedside.Annals of hematology · 2026Review
- MHC1-TIP enables single-tube multimodal immunopeptidome profiling and uncovers intratumoral heterogeneity in antigen presentation.Communications biology · 2026Article
- Phosphorylation shapes antigen presentation and immune recognition: mechanistic insights and translational perspectives.Frontiers in immunology · 2026Review
- Small Molecule Modulation of MHC-I Surface Expression: A Click Chemistry-Based Discovery Approach.Journal of medicinal chemistry · 2025Article
- Rapid and direct discovery of functional tumor specific neoantigens by high resolution mass spectrometry and novel algorithm prediction.Cell insight · 2025Article
- Framework for analyzing MAE-derived immunopeptidomes from cell lines with shared HLA haplotypes.PloS one · 2025Article
- Unlocking the secrets of the immunopeptidome: MHC molecules, ncRNA peptides, and vesicles in immune response.Frontiers in immunology · 2025Review
- Crucial Parameters for Immunopeptidome Characterization: A Systematic Evaluation.International journal of molecular sciences · 2024Article
- Immunogenicity of Non-Mutated Ovarian Cancer-Specific Antigens.Current oncology (Toronto, Ont.) · 2024Article
- Gemcitabine Modulates HLA-I Regulation to Improve Tumor Antigen Presentation by Pancreatic Cancer Cells.International journal of molecular sciences · 2024Article
- COSMIC-based mutation database enhances identification efficiency of HLA-I immunopeptidome.Journal of translational medicine · 2024Article
- Immune Surveillance of Acute Myeloid Leukemia Is Mediated by HLA-Presented Antigens on Leukemia Progenitor Cells.Blood cancer discovery · 2023Article
- Unlocking the potential of microfluidics in mass spectrometry-based immunopeptidomics for tumor antigen discovery.Cell reports methods · 2023Review
- Proteomic discovery of chemical probes that perturb protein complexes in human cells.Molecular cell · 2023Article
- NLRC5-CIITA Fusion Protein as an Effective Inducer of MHC-I Expression and Antitumor Immunity.International journal of molecular sciences · 2023Article
- Novel canonical and non-canonical viral antigens extend current targets for immunotherapy of HPV-driven cervical cancer.iScience · 2023Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To understand and treat immunology-related diseases, a comprehensive, unbiased characterization of major histocompatibility complex (MHC) peptide ligands is of key importance. Preceding the analysis by mass spectrometry, MHC class I peptide ligands are typically isolated by MHC immunoaffinity chromatography (MHC-IAC) and less often by mild acid elution (MAE). MAE may provide a cheap alternative to MHC-IAC for suspension cells but has been hampered by the high number of contaminating, MHC-unrelated peptides. Here, we optimized MAE, yielding MHC peptide ligand purities of more than 80%. When compared with MHC-IAC, obtained peptides were similar in numbers, identities, and to a large extent intensities, while the percentage of cysteinylated peptides was 5 times higher in MAE. The latter benefitted the discovery of MHC-allotype-specific, distinct cysteinylation frequencies at individual positions of MHC peptide ligands. MAE revealed many MHC ligands with unmodified, N-terminal cysteine residues which get lost in MHC-IAC workflows. The results support the idea that MAE might be particularly valuable for the high-confidence analysis of post-translational modifications by avoiding the exposure of the investigated peptides to enzymes and reactive molecules in the cell lysate. Our improved and carefully documented MAE workflow represents a high-quality, cost-effective alternative to MHC-IAC for suspension cells.
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