In collaboration with the team of J-P Girard at IPBS, we use proteomic analysis associated with label-free quantification to study inflammatory mechanisms, particularly the mode of action of Interleukin-33 (IL-33), a nuclear cytokine involved in type 2 immunity, inflammation and allergy.
More than 10 years ago, we developed original bioinformatics tools to extract peptide signals from raw MS files, measure their intensity, and perform quantitative analysis of protein expression in large-scale studies. Using such methods, we could extensively map at that time the response of human endothelial cells to several inflammatory cytokines, such as TNFα, IFNg and IL1β (1,2).
We keep on applying such a global proteomic approaches to analyze IL-33 function in endothelial cells and other target immune cells such as group 2 innate lymphoid cells (ILC2s), which play an important role in asthma.
We use large-scale protein profiling to compare the extracellular and intracellular activity of IL-33 in primary human endothelial cells (3). Using highly sensitive mass spectrometry, we could also identify the cleavage sites generated on IL-33 by a whole panel of allergens. These cleavage events induce activation of the cytokine, finally triggering asthma (4,5).