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Sub‐proteome analysis of novel IgE‐binding proteins from Bermuda grass pollen
Author(s) -
Kao ShaoHsuan,
Su SongNan,
Huang ShihWen,
Tsai JawJi,
Chow LuPing
Publication year - 2005
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200401229
Subject(s) - proteome , immunoglobulin e , allergen , pollen , cynodon dactylon , biology , immunology , allergy , antibody , chemistry , biochemistry , botany
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.