|Title:||Characterization of a Novel Allergen, a Major Ige-Binding Protein from Aspergillus Flavus, as an Alkaline Serine Protease||Authors:||Yu, Chia-Jung
|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.
|Appears in Collections:||醫學系|
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