Immune peptides are presented by major histocompatibility complex (MHC) class I and II complexes at the surface of cells and are recognized by T cell receptors.
Presentation of an aberrant immune peptide at the surface of the cell will lead to stimulation of the adaptive immune system. These aberrant immune peptides are thus critical for several biological processes. For example, neoantigens are immunopeptides derived from somatic mutations and are crucial for the recognition of cancer cells by T-cells. The identification of such neoantigens is essential for developing novel cancer immunotherapies. Also, the presentation of antigens originating from bacteria or viruses that will lead to the induction of an adaptive immune response against these bacteria, viruses and their infected cells are crucial for development of vaccines. Additionally, measuring whether admission of a protein drug will lead to an unintended immune response and pinpointing the responsible immune peptide is key in preclinical phases of drug development.
We optimized methods to identify immune peptides from human and murine samples. By immune-purification of MHC type I and/or type II complexes, respectively presenting immune peptides originating from inside the cell (in all cells) or originating from outside the cell (in professional antigen presenting cells) followed by the identification of their immune peptides by mass spectrometry we can pinpoint the peptides responsible for the resulting immune response. This identification of immune peptides will drive research and development of protein drugs forward.