Evidence for Novel Tomato Seed Allergens: IgE-Reactive Legumin and Vicilin Proteins Identified by Multidimensional Protein Fractionation-Mass Spectrometry and in Silico Epitope Modeling

被引:32
作者
Baessler, Olivia Y. [1 ]
Weiss, Julia [2 ]
Wienkoop, Stefanie [2 ]
Lehmann, Karola [3 ]
Scheler, Christian [3 ]
Doelle, Sabine [4 ]
Schwarz, Dietmar [5 ]
Franken, Philipp [5 ]
George, Eckhard [5 ]
Worm, Margitta [4 ]
Weckwerth, Wolfram [1 ,2 ]
机构
[1] Max Planck Inst Mol Plant Physiol, D-14467 Potsdam, Germany
[2] Univ Potsdam, GoFORSYS, D-14467 Potsdam, Germany
[3] Proteome Factory AG, D-10117 Berlin, Germany
[4] Allergie Ctr Charite, Dept Dermatol & Allergy, D-10117 Berlin, Germany
[5] Leibniz Inst Vegetable & Ornamental Crops IGZ, D-14979 Grossbeeren, Germany
关键词
food allergy; tomato; legumin; vicilin; IgE; mass spectrometry; LC-MS/MS; immunoblot; QUANTITATIVE SHOTGUN PROTEOMICS; ANACARDIUM-OCCIDENTALE L; PLANT FOOD ALLERGENS; ARA H 1; CROSS-REACTIVITY; ARABIDOPSIS-THALIANA; MUTATIONAL ANALYSIS; BINDING EPITOPES; AMINO-ACID; LATEX;
D O I
10.1021/pr800186d
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Tomato fruit and seed allergens were detected by IgE-immunoblotting using sera from 18 adult tomato-sensitized patients selected based on a positive history skin prick test (SPT) and specific Immunglobulin (Ig) E-levels. Isolated tomato seed total protein showed high SPT activity comparable or even higher than tomato fruit protein. For the molecular characterization of tomato seed allergens, a multidimensional protein fractionation strategy and LC-MS/MS was used. Two legumin- and vicilin-proteins were purified and showed strong IgE-reactivity in immunoblots. Individual patient sera exhibited varying IgE-sensitivity against the purified proteins. In silico structural modeling indicates high homology between epitopes of known walnut allergens and the detected IgE-crossreactive tomato proteins.
引用
收藏
页码:1111 / 1122
页数:12
相关论文
共 45 条
[1]  
ALCALA JVJ, 2000, GENERATION EST UNPUB
[2]  
[Anonymous], 2001, REP JOINT FAO WHO EX
[3]   Detection of clinical markers of sensitization to profilin in patients allergic to plant-derived foods [J].
Asero, R ;
Mistrello, G ;
Roncarolo, D ;
Amato, S ;
Zanoni, D ;
Barocci, F ;
Caldironi, G .
JOURNAL OF ALLERGY AND CLINICAL IMMUNOLOGY, 2003, 112 (02) :427-432
[4]   Latex allergy can induce clinical reactions to specific foods [J].
Beezhold, DH ;
Sussman, GL ;
Liss, GM ;
Chang, NS .
CLINICAL AND EXPERIMENTAL ALLERGY, 1996, 26 (04) :416-422
[5]  
BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
[6]  
Breiteneder H, 2004, J ALLERGY CLIN IMMUN, V113, P821, DOI [10.1016/j.jaci.2004.01.079, 10.1016/j.jaci.2004.01.779]
[7]   Biological master games: Using biologists' reasoning to guide algorithm development for integrated functional genomics [J].
Breitling, R ;
Herzyk, P .
OMICS-A JOURNAL OF INTEGRATIVE BIOLOGY, 2005, 9 (03) :225-232
[8]   Mapping and mutational analysis of the IgE-binding epitopes on Ara h 1, a legume vicilin protein and a major allergen in peanut hypersensitivity [J].
Burks, AW ;
Shin, D ;
Cockrell, G ;
Stanley, JS ;
Helm, RM ;
Bannon, GA .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1997, 245 (02) :334-339
[9]  
DEMARTINO M, 1988, ALLERGY, V43, P206
[10]   Cross-reactions in the latex-fruit syndrome: A relevant role of chitinases but not of complex asparagine-linked glycans [J].
Diaz-Perales, A ;
Collada, C ;
Blanco, C ;
Sanchez-Monge, R ;
Carrillo, T ;
Aragoncillo, C ;
Salcedo, G .
JOURNAL OF ALLERGY AND CLINICAL IMMUNOLOGY, 1999, 104 (03) :681-687