Peanut allergen Ara h 3: Isolation from peanuts and biochemical characterization

被引:148
作者
Koppelman, SJ
Knol, EF
Vlooswijk, RAA
Wensing, M
Knulst, AC
Hefle, SL
Gruppen, H
Piersma, S
机构
[1] TNO, Nutr & Food Res Inst, Dept Protein Technol, NL-3700 AJ Zeist, Netherlands
[2] Univ Utrecht, Med Ctr, Dept Dermatol Allergol, Utrecht, Netherlands
[3] TNO WU, Ctr Prot Technol, Wageningen, Netherlands
[4] Univ Nebraska, Food Allergy Res & Resource Program, Lincoln, NE USA
[5] Univ Wageningen & Res Ctr, Dept Agrotechnol & Food Sci, Wageningen, Netherlands
关键词
allergens; IgE-binding; peanut; purification;
D O I
10.1034/j.1398-9995.2003.00259.x
中图分类号
R392 [医学免疫学];
学科分类号
100102 ;
摘要
Background: Peanut allergen Ara h 3 has been the subject of investigation for the last few years. The reported data strongly depend on recombinant Ara h 3, since a purification protocol for Ara h 3 from peanuts was not available. Methods: Peanut allergen Ara h 3 (glycinin), was purified and its posttranslational processing was investigated. Its allergenic properties were determined by studying IgE binding characteristics of the purified protein. Results: Ara h 3 consists of a series of polypeptides ranging from approximately 14 to 45 kDa that can be classified as acidic and basic subunits, similar to the subunit organization of soy glycinin. N-terminal sequences of the individual polypeptides were determined, and using the cDNA deduced amino-acid sequence, the organization into subunits was explained by revealing posttranslational processing of the different polypeptides. IgE-binding properties of Ara h 3 were investigated using direct elisa and Western blotting with sera from peanut-allergic individuals. The basic subunits, and to a lesser extent the acidic subunits, bind IgE and may act as allergenic peptides. Conclusions: We conclude that peanut-derived Ara h 3, in contrast to earlier reported recombinant Ara h 3, resembles, to a large extent, the molecular organization typical for proteins from the glycinin family. Furthermore, posttranslational processing of Ara h 3 affects the IgE-binding properties and is therefore an essential subject of study for research on the allergenicity of Ara h 3.
引用
收藏
页码:1144 / 1151
页数:8
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