Soy allergy in perspective
The purpose of this paper is to review and discuss studies on soy allergy.
In Central Europe soy is a clinically relevant birch pollen-related allergenic food. Crossreaction is mediated by a Bet v 1 homologous protein, Gly m 4. Additionally, birch pollen allergic patients might acquire through Bet v 1 sensitization allergies to mungbean or peanut, in which Vig r 1 and Ara h 8 are the main cross-reactive allergens. Threshold doses in soy allergic individuals range from 10 mg to 50 g of soy and are more than one order of magnitude higher than in peanut allergy. No evidence was found for increased allergenicity of genetically modified soybeans.
In Europe, both primary and pollen-related food allergy exist. The diagnosis of legume allergy in birch pollen-sensitized patients should not be excluded on a negative IgE testing to legume extracts. Bet v 1 related allergens are often underrepresented in extracts. Gly m 4 from soy and Ara h 8 from peanut are nowadays commercially available and are recommended in birch pollen allergic patients with suspicion of soy or peanut allergy, but negative extract-based diagnostic tests to screen for IgE specific to these recombinant allergens.
Available from: Tatiana Cucu
- "Soybeans (Glycine max) contain about 35% of proteins and at least 21 proteins have been shown to be IgE-reactive. Soybean allergy can occur as a result of primary sensitization, 28 but can also be related to birch pollen allergy through structural similarities between the birch pollen allergen Bet v 1 and the corresponding protein Gly m 4 in soybeans (secondary allergy) 30 (Ballmer-Weber and Vieths 2008; Mittag et al. 2004). The symptoms associated with soybean allergy are mostly mild, such as the Oral Allergy Syndrome (OAS), however, severe reactions 32 have also been described (Foucard and Yman 1999; Kleine-Tebbe et al. 2002; Mittag et al. 2004). "
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ABSTRACT: Soybean (Glycine max) is the world's primary provider of protein and oil and is widely used in foodstuffs. However, the use of soybean in foodstuffs might pose a serious threat to allergic consumers since some proteins can cause allergic reactions. To date mostly ELISA methods are used for testing contamination of foodstuffs with soybean. In view of the complexity regarding allergen detection in foodstuffs and appropriate food product labelling, the aim of this study was to investigate the impact of the Maillard reaction on the detectability of soybean proteins using commercial ELISA kits. Accumulation of protein-bound carbonyls, modification of reactive lysine residues and severe aggregation as a result of incubation with glucose, in the presence or absence of soluble wheat proteins, were recorded. Moreover, detection of soybean proteins by means of three commercial ELISA kits was strongly altered and was highly dependent on the type of kit used.
Food Additives and Contaminants - Part A Chemistry, Analysis, Control, Exposure and Risk Assessment 02/2011; 28(2):127-35. DOI:10.1080/19440049.2010.539627 · 1.80 Impact Factor
Available from: Michael Hauser
- "The individual profilins and members of the Bet v 1 allergen family (PR-10 proteins) listed in the table have been convincingly demonstrated to be of clinical relevance in ragweed, timothy grass, and birch pollinosis-associated food allergies [3,5,12,13] by in vivo (SPT) or in vitro (mediator release) assays [5,7,26,74-77]. A picture is now emerging in which profilins seem to be responsible for pollinosis-associated allergy to non-Rosaceae fruits (ragweed Amb a 8 and timothy grass Phl p 12). PR-10 proteins (Bet v 1) and to a minor extent profilins (Bet v 2) appear to be involved in food incompatibilities associated with birch pollinosis. "
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ABSTRACT: The panallergen concept encompasses families of related proteins, which are involved in general vital processes and thus, widely distributed throughout nature. Plant panallergens share highly conserved sequence regions, structure, and function. They are responsible for many IgE cross-reactions even between unrelated pollen and plant food allergen sources. Although usually considered as minor allergens, sensitization to panallergens might be problematic as it bears the risk of developing multiple sensitizations. Clinical manifestations seem to be tightly connected with geographical and exposure factors. Future population- and disease-based screenings should provide new insights on panallergens and their contribution to disease manifestations. Such information requires molecule-based diagnostics and will be valuable for developing patient-tailored prophylactic and therapeutic approaches. In this article, we focus on profilins, non-specific lipid transfer proteins, polcalcins, and Bet v 1-related proteins and discuss possible consequences of panallergen sensitization for the allergic patient. Based on their pattern of IgE cross-reactivity, which is reflected by their distribution in the plant kingdom, we propose a novel classification of panallergens into ubiquitously spread "real panallergens" (e.g. profilins) and widespread "eurallergens" (e.g. polcalcins). "Stenallergens" display more limited distribution and cross-reactivity patterns, and "monallergens" are restricted to a single allergen source.
Allergy Asthma and Clinical Immunology 01/2010; 6(1):1. DOI:10.1186/1710-1492-6-1 · 2.03 Impact Factor
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ABSTRACT: Wir berichten über einen Patienten mit einer selten auftretenden anaphylaktischen Reaktion nach dem Verzehr roher Paprika.
Die allergologische Diagnostik zeigte ein komplexes Sensibilisierungsmuster, u.a. auf Gräser und Birke mit Hinweisen auf
eine pollenassoziierte Nahrungsmittelallergie. Am ehesten führen wir die Reaktion auf eine Bet-v-1-bedingte Kreuzreaktion
zurück. Im Westernblot zeigte sich eine Bindung des Patientenserums an ein 11-kDa-Protein, bei dem es sich möglicherweise
um ein bisher unbekanntes Allergen der Paprikapflanze handelt oder um ein Fragment des Bet-v-1-homologen Paprikaproteins.
We report on a patient with rare anaphylaxis after ingestion of raw bell pepper. A complex cluster of sensitization including
grass and birch pointed out a possible pollen-associated food allergy. We suggest that the severe reaction is due to cross-reactivity
towards Betv1. Western blot showed binding of the patient’s serum to an 11kDa protein, which has not been described yet
and might be a new allergenic structure of the bell pepper plant or a fragment of the Betv1-homologous bell pepper protein.
KeywordsBell pepper-Anaphylaxis-Food allergy-Betv1-11kDa protein
Der Hautarzt 04/2009; 61(4):339-342. DOI:10.1007/s00105-009-1776-3 · 0.56 Impact Factor
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