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Secretome analysis of novel IgE-binding proteins from Penicillium citrinum
Li-Li Chiu1, Kuang-Lun Lee, Yu-Fen Lin
1Graduate Institute of Biochemistry and Molecular Biology, College of Medicine, National Taiwan University, Taipei, Taiwan.
Abstract:
The Penicillium genus of fungi is a frequently reported cause of allergic reactions. However, only a limited number of allergens have been reported. In Penicillium spp., many allergens show higher IgE-binding activity in culture filtrate extracts than in cellular extracts. In order to investigate the IgE-reactive profile of mold-sensitized patients, secreted IgE-reactive proteins from Penicillium citrinum were identified by 2-DE, serum immunoblotting, and nanoLC-MS/MS. Among the IgE-reactive spots, one known allergen, Pen c 13, and four novel allergens were identified. The cDNAs coding for Pen c 32 and Pen c 30 were cloned using designed primers based on nanoLC-MS/MS analysis. The amino acid sequences of Pen c 32 and Pen c 30 were, respectively, found to have extensive similarity with those of pectate lyases and catalases from various fungi. Native Pen c 30 was shown to have catalase activity and to bind to serum IgE from 48% of mold-allergic patients and induced immediate type skin reactions in a sensitized patient. Here, we present a proteome approach which resulted in the identification of four novel secreted allergens. These novel allergens might be useful in allergy diagnosis and in the treatment of mold-allergic disorders.
Insights
Researchers identified four new secreted allergens from Penicillium citrinum, a common mold causing allergies. These novel mold allergens could improve allergy diagnosis and treatments for mold-allergic patients.
Area of Science:
- Mycology
- Allergology
- Proteomics
Background:
- The Penicillium genus is a common cause of allergic reactions.
- Limited allergens identified in Penicillium species, with many found in culture filtrate.
- Investigating IgE-binding proteins is crucial for understanding mold allergy.
Purpose of the Study:
- To identify secreted IgE-reactive proteins from Penicillium citrinum.
- To characterize novel allergens for potential diagnostic and therapeutic applications.
- To explore the IgE-reactive profile in mold-sensitized individuals.
Main Methods:
- Proteomic analysis using 2-DE, serum immunoblotting, and nanoLC-MS/MS.
- Cloning of cDNAs for novel allergens Pen c 32 and Pen c 30.
- Biochemical assays to determine enzyme activity and IgE-binding capacity.
Main Results:
- Identification of one known allergen (Pen c 13) and four novel secreted allergens.
- Pen c 32 and Pen c 30 showed sequence similarity to pectate lyases and catalases.
- Native Pen c 30 exhibited catalase activity and IgE binding in 48% of mold-allergic patients, inducing skin reactions.
Conclusions:
- A proteomic approach successfully identified four novel secreted allergens from Penicillium citrinum.
- These novel allergens, particularly Pen c 30, are significant triggers of allergic reactions.
- The identified allergens hold potential for improving allergy diagnosis and treatment strategies for mold allergies.
