Molecular Cloning and Immunochemical Characterization of a New Japanese Cedar Pollen Allergen Homologous to Plant Subtilisin-Like Serine Protease

Protease activities in allergen sources are thought to be involved in triggering allergic inflammation through the disruption of epithelial barrier or the induction of proinflammatory cytokines. Protease allergens may also work as type 2 helper T cell (T.sub.H 2) adjuvants through the cleavage of ce...

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Bibliographic Details
Published in:The World Allergy Organization journal 2010-11, Vol.3 (11), p.262-265
Main Authors: Nour Ibrahim, Ahmed Ragaa, Kawamoto, Seiji, Mizuno, Keisuke, Shimada, Yayoi, Rikimaru, Satoshi, Onishi, Nobukazu, Hashimoto, Kunihiko, Aki, Tsunehiro, Hayashi, Takaharu, Ono, Kazuhisa
Format: Article
Language:English
Subjects:
Allergens
Allergic reaction
Allergy
Cytokines
Immunoglobulin E
Original Research
Serine
Thrombin
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Summary:Protease activities in allergen sources are thought to be involved in triggering allergic inflammation through the disruption of epithelial barrier or the induction of proinflammatory cytokines. Protease allergens may also work as type 2 helper T cell (T.sub.H 2) adjuvants through the cleavage of cell surface receptors. Here, we report molecular cloning and immunochemical characterization of a new Japanese cedar (Cryptomeria japonica) pollen allergen (CPA9) homologous to serine protease, which is initially found as a high IgE-binding spot on our two-dimensional (2-D) IgE immunoblotting map. The cpa9 cDNA encoded a 757 amino acid polypeptide showing a significant sequence identity with plant subtilisin-like serine protease family members including melon major allergen Cuc m 1. We found that native CPA9 purified from C. japonica pollen showed a high IgE-binding frequency and IgE cross-reactivity with melon extract.
ISSN:1939-4551
1939-4551
DOI:10.1097/WOX.0b013e318201d81d