국내산 중하(Metapenaeus joyneri)내 주요 알레르겐 규명: 가열 및 소화액에 의한 변화
Identification of the Major Allergen in the Shrimp (Metapenaeus Joyneri): Effects of Heating and Digestive Enzymes
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Abstract
Background: Shrimp is one of the major causative food allergens in this country. We reported IgE-prevalence and its IgE binding components of the home made shrimp (M. joyneri) extracts in allergy patients in this country. The Property of food allergens can be changed by heat or digestion enzymes. We observed the changes of IgE binding components of Metapenaeus joyneri with exposure to heating and digestive enzymes in ex vivo system. Method: IgE immunoblot was applied to analyze the changes of IgE binding components within the fresh and boiled shrimps in sera from five patients with allergy showing strong positive reactions (A/H ≥2+) to the skin prick test and high serum specific IgE (≥100 A.U) to the shrimp. To evaluate heating and enzyme effects, heating, SGF (gastric fluid, simulated) and SIF (intestinal fluid, simulated) were treated for 10, 30 and 90 minutes and SDS-PAGE and IgE-immunoblot were repeated. To identify the major allergens, 2-D electrophoresis and IgE-immunoblot were followed by amino acid sequence analysis using MALDI-TOF and FASTF program. Result: The 45 kDa band was resistant to heating in three of five patients. In the fresh shrimp, 36～45 kDa bands remained after SGF treatment, while minimal changes were noted after SIF treatment. The 2D-immunoblot of 45 kDa demonstrated two spots (pI 5.1, 4.75), and one (pI 5.1) was identified as an arginine kinase having 100% homology with European lobster by amino acid analysis. Conclusion: The major allergen of M. joyneri was identified as an arginine kinase which was resistant to heating and digestion enzymes.
참고문헌 (21)
- "IgE reactivity against a cross-reactivity allergy in crustacea and mollusca: Evidence for Tropomyosin as the common allergen.", 98, pp.954~961 (1996)
- "Molecular characterization of American cockroach Tropomyosin", 162, pp.4342~4348 (1999)
- "The major heat stable allergen of shrimp", pp.17~22
- "expression and primary structure of Metapenaeus ensis tropomyosin", pp.882~90
- "Identification of the major brown shrimp allergen as the muscle protein tropomyosin", pp.49~55
- , jallergyclinimmunol1991, ~
- "Proteomics and immunological analysis of a novel shrimp allergen, Pen m 2.", 170, pp.445~453 (2003)
- "Evolution of phosphagen kinase Amino acid sequence of arginine kinase from the shrimp Penaeus japonicus", pp.229~34
- "Trypanosoma cruzi arginine kinase characterization and cloning.", 275, pp.1495~1501 (2000)
- "Arginine kinase is highly expressed in the compound eye of the honey bee, Apis mellifera.", 211, pp.343~349 (1998)
- "Cloning and sequence analysis of the cDNA for arginine kinase of lobster muscle", pp.21599~605
- "Digestibility of allergens extracted from natural rubber latex and vegetable foods.", 106, pp.752~762 (2000)
- "Specific IgE determination to shrimp (Metapenaeus joyneri) and identification of its allergen.", 65, pp.231~238 (2003)
- "Isolation and characterization of heat-stable allergens from shrimp", pp.26~36
- "Identification of B cell epitopes with shrimp specific monoclonal antibodies Molecular biology and immunology of allergens", pp.~294 (1993)
- "Expression of arginine kinase enzymatic activity and mRNA in gills of the euryhaline crabs Carcinus maenas and Callinectes sapidus.", 203, pp.2395~2404 (2000)
- "Molecular and immunological characterization of arginine kinase from the Indianmeal moth, Plodia interpunctella, a novel cross-reactive invertebrate pan-allergen.", 167, pp.5470~5477 (2001)
- "Evaluation of the impact of food technology on the allergenicity of cow's milk proteins.", 58, pp.587~592 (1999)
- "Boletus edulis: a digestion-resistant allergen may be relevant for food allergy.", 32, pp.771~775 (2002)
- "Cross-reactivity between fruit and vegetables", 31, pp.141~146 (2003)
- "Cross-reactivity of IgE-binding components between boiled Atlantic shrimp and German cockroach", 50, pp.918~924 (1995)