https://scholars.lib.ntu.edu.tw/handle/123456789/194889
Title: | Characterization of a Novel Allergen, a Major Ige-Binding Protein from Aspergillus Flavus, as an Alkaline Serine Protease | Authors: | Yu, Chia-Jung Chiou, Shyh-Horng Lai, Wei-Yu Chiang, Bor-Luen Chow, Lu-Ping |
Keywords: | mold allergens;IgE-binding activity;alkaline serine protease;Aspergillus flavus;CDNA CLONE;FUMIGATUS | Issue Date: | 1999 | Journal Volume: | v.261 | Journal Issue: | 675 | Start page/Pages: | - | Source: | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | Abstract: | Aspergillus species of fungi have been known to be one of the most prevalent aeroallergens. One important A flavus allergen (Asp fl 1) was identified by means of immunoblotting with a serum pool of allergic patients on a two-dimensional electrophoretic gel. The cDNA coding for Asp fl 1 was cloned and sequenced. The clone encodes a full- length protein of 403 amino acid precursors of 42 kDa. After cleavage of a putative signal peptide of 21 amino acids and a prepeptide of 100 amino acids, a mature protein of 282 amino acids was obtained with a molecular mass of 33 kDa and a pi of 6.3, A degree of identity was found in a range of 27 to 84% among related allergens derived from bacteria allergen subtilisin, mold allergen Pen c 1, and virulence factor of A. fumigatus. Recombinant Asp fl 1 (rAsp fl 1) was cloned into vector pQE-30 and expressed in E. coli M15 as a histidine-tag fusion protein and purified to homogeneity, The IgE binding capacity of rAsp fi 1 was tested by immunoblotting using a serum pool of Aspergillus-allergic patients. Recombinant allergen cross- reacted strongly with IgE specific for natural Asp fl 1 and Pen c 1, indicating that common IgE epitopes may exist between allergens of A. flavus and P. citrinum. (C) 1999 Academic Press. |
URI: | http://ntur.lib.ntu.edu.tw//handle/246246/94781 |
Appears in Collections: | 醫學系 |
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