The human eosinophil proteome. Changes induced by birch pollen allergy.

Proteins from human eosinophils were separated bidimensionally and identified by mass spectrometry (336 spots/bands, 98 different proteins). Of these, 24.7% belonged to the cytoskeleton/migration group. Highly basic proteins (11.3%) were concentrated in the granule-containing cell fraction. We detected novel hyperacidic forms of cofilin-1, profilin-1 and adenylyl cyclase-associated protein, and hyperbasic forms of eosinophil-derived neurotoxin/eosinophil protein X and major basic protein homologue. We also found evidence of the triglycosylation of the heavy chain of eosinophil peroxidase. In addition, through comparative 2D image analysis, spot quantification and MS, it was found that hsc70, actin-capping protein and hyperacidic forms of eosinophil peroxidase heavy chain are overexpressed in cells from birch pollen allergic subjects, at the peak of a season. The link between these findings and an increased cellular antigen-presenting capacity and motility are discussed.