The Human Eosinophil Proteome. Changes Induced by Birch Pollen Allergy

Abstract

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.

Exosomes from eosinophils autoregulate and promote eosinophil functions

“…In previously published proteomic studies, the number of proteins identified varied from 98 to 500 [28], but those proteins corresponded with the complete eosinophil proteome, not with the exosomederived proteome. Our results verified the presence of several previously described exosome-associated proteins from different sources as well as specific eosinophil proteins [28,29]. Exosome content varied depending on the cellular sources, and it is, thus, reasonable to expect that exosomes derived from different cells will have specific effects on the target cells.…”

Altered Eosinophil Proteome in a Patient with Hypereosinophilia from Acute Fascioliasis

“…Further studies using more patients are planned to evaluate phosphorylation of eosinophil proteins as a result of Fasciola infection. Proteomic studies of circulating eosinophils from patients with atopic dermatitis or pollen allergy did not correlate well with each other or the current study (12,13). This suggests that the eosinophil proteome may differ depending on the route of sensitization or the allergen, even in patients with eosinophilia.…”

Toward the proteome of the human peripheral blood eosinophil

“…Waschnagg et al . [12] very recently evaluated protein expression differences induced by Birch pollen allergy and identified 97 unique non-redundant eosinophil proteins of which 90 occur in our list of 426 (Table 1) which is an excellent agreement. However, a comparative proteomic study of healthy versus atopic dermatitis patients identified 51 differentially expressed proteins of which only three are included in Table 1 [13].…”