Secretome analysis of novel IgE-binding proteins from Penicillium citrinum

  • Chiu L
  • Lee K
  • Lin Y
 et al. 
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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.

Author-supplied keywords

  • Immunoglobulin E-reactive protein
  • Pen c 30
  • Pen c 32
  • Penicillium citrinum
  • Secretome

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Authors

  • Li Li Chiu

  • Kuang Lun Lee

  • Yu Fen Lin

  • Chia Yu Chu

  • Son Nan Su

  • Lu Ping Chow

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