title: Sub-proteome analysis of novel IgE-binding proteins from Bermuda grass pollen.
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.
authors.affiliation: Institute of Biochemistry and Molecular Biology, College of Medicine, National Taiwan University, Taipei, Taiwan.
authors.forename: Shao-Hsuan
authors.initials: SH
authors.lastname: Kao
authors.forename: Song-Nan
authors.initials: SN
authors.lastname: Su
authors.forename: Shih-Wen
authors.initials: SW
authors.lastname: Huang
authors.forename: Jaw-Ji
authors.initials: JJ
authors.lastname: Tsai
authors.forename: Lu-Ping
authors.initials: LP
authors.lastname: Chow
mesh_terms: D015153:Blotting, Western; D031744:Cynodon / Q000737:chemistry*; D007073:Immunoglobulin E / Q000378:metabolism*; D010940:Plant Proteins / Q000737:chemistry* / Q000378:metabolism; D020543:Proteome; D021241:Spectrometry, Mass, Electrospray Ionization; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D010940:Plant Proteins; D020543:Proteome; D007073:Immunoglobulin E