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    Area of Science:

    • Immunology
    • Biochemistry
    • Proteomics

    Background:

    • Adaptive immunity relies on Major Histocompatibility Complex class I (MHC-I) presenting antigenic peptides to cytotoxic T-cells.
    • Peptide selection for MHC-I presentation normally ensures self-tolerance, but chemical modifications can interfere.
    • Post-translational modifications (PTMs) and non-enzymatic changes alter peptide structure, potentially affecting immune recognition.

    Purpose of the Study:

    • To investigate the impact of non-enzymatic PTMs on antigen presentation and T cell recognition.
    • To understand how these modifications affect the cancer-associated immunopeptidome.

    Main Methods:

    • Synthesis of peptide variants with common non-enzymatic PTMs using the SIINFEKL model epitope.
    • Assessment of modified peptides' effects on MHC-I binding affinity and T cell recognition.
    • Development of an alkyne-modified probe for enrichment and identification of non-enzymatically acylated peptides.

    Main Results:

    • Non-enzymatic PTMs significantly alter peptide affinity for MHC-I molecules.
    • These modifications were shown to impact the cancer-associated immunopeptidome.
    • A novel method was established to identify sites of non-enzymatic acylation relevant to MHC-I display.

    Conclusions:

    • Non-enzymatic PTMs are critical modulators of the immunopeptidome.
    • These modifications play a significant role in shaping adaptive immune responses.
    • Understanding these chemical alterations is crucial for cancer immunology and immunotherapy.