Sub-proteome analysis of novel IgE-binding proteins from Bermuda grass pollen
Journal
Proteomics
Journal Volume
5
Journal Issue
14
Pages
3805-3813
Date Issued
2005
Author(s)
Abstract
Bermuda grass (Cynodon dactylon) pollen (BGP) is one of the most common causes of airway allergic disease, and has been shown to contain over 12 allergenic proteins on 1-D immunoglobulin E (IgE) immunoblots. However, only a few allergens have been identified and characterized. Cyn d 1 is a major allergen and the most abundant protein in BGP, representing 15% of the whole-pollen extract. To investigate variability in the IgE-reactive patterns of BGP-sensitized patients and to identify other prevalent allergens, a BGP extract was passed through an affinity column to remove Cyn d 1, and the non-bound material was collected and analyzed by 2-DE. IgE-reactive proteins were subsequently characterized by immunoblotting using serum samples from ten BGP-allergic patients. The prevalent IgE-reactive proteins were identified by MALDI-TOF MS, N-terminal sequence similarity, and LC-MS/MS. Here, we present a sub-proteome approach for allergen investigation and its use for determining BGP 2-DE profiles and identifying six novel allergens. ? 2005 Wiley-VCH Verlag GmbH & Co. KGaA.
SDGs
Other Subjects
allergen; binding protein; immunoglobulin E; proteome; article; binding affinity; controlled study; grass pollen; human; immunoblotting; liquid chromatography; matrix assisted laser desorption ionization time of flight mass spectrometry; priority journal; protein analysis; proteomics; tandem mass spectrometry; two dimensional electrophoresis; Blotting, Western; Cynodon; Immunoglobulin E; Plant Proteins; Proteome; Spectrometry, Mass, Electrospray Ionization; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Cynodon dactylon
Type
journal article