Our deep coverage and quantitative analyses fill an important gap in the existing maps of the human proteome and will enable the strategic use of proteomics to study eosinophils in human diseases.Īcquiring deep proteomic coverage through mass spectrometry (MS)-based analysis can aid understanding of system-wide processes, confirm expression of transcripts, inform experiments of specific proteins and protein complexes of particular interest, and generate hypotheses about pathways altered in disease. We account for the contribution of platelets that routinely contaminate purified eosinophils and report the variability in the eosinophil proteome among five individuals and proteomic changes accompanying acute activation of eosinophils by interleukin-5. Our analysis yielded 100,892 unique peptides mapping to 7,086 protein groups representing 6,813 genes as well as 4,802 site-specific phosphorylation events. We now report a map of the nonstimulated peripheral blood eosinophil proteome assembled using two-dimensional liquid chromatography coupled with high-resolution mass spectrometry. The proteome of the eosinophil is largely unannotated with under 500 proteins identified. The eosinophil is a type of granulocytic leukocyte specified early in hematopoietic differentiation that participates in barrier defense, innate immunity, and allergic disease. A system-wide understanding of biological processes requires a comprehensive knowledge of the proteins in the biological system.
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