Commins SP, Satinover SM, Hosen J, et al. Delayed anaphylaxis, angioedema, or urticaria after consumption of red meat in patients with IgE antibodies specific for galactose-alpha-1,3-galactose

Asthma and Allergic Diseases Center, University of Virginia Health System, Charlottesville, VA, USA.
The Journal of allergy and clinical immunology (Impact Factor: 11.48). 02/2009; 123(2):426-33. DOI: 10.1016/j.jaci.2008.10.052
Source: PubMed


Carbohydrate moieties are frequently encountered in food and can elicit IgE responses, the clinical significance of which has been unclear. Recent work, however, has shown that IgE antibodies to galactose-alpha-1,3-galactose (alpha-gal), a carbohydrate commonly expressed on nonprimate mammalian proteins, are capable of eliciting serious, even fatal, reactions.
We sought to determine whether IgE antibodies to alpha-gal are present in sera from patients who report anaphylaxis or urticaria after eating beef, pork, or lamb.
Detailed histories were taken from patients presenting to the University of Virginia Allergy Clinic. Skin prick tests (SPTs), intradermal skin tests, and serum IgE antibody analysis were performed for common indoor, outdoor, and food allergens.
Twenty-four patients with IgE antibodies to alpha-gal were identified. These patients described a similar history of anaphylaxis or urticaria 3 to 6 hours after the ingestion of meat and reported fewer or no episodes when following an avoidance diet. SPTs to mammalian meat produced wheals of usually less than 4 mm, whereas intradermal or fresh-food SPTs provided larger and more consistent wheal responses. CAP-RAST testing revealed specific IgE antibodies to beef, pork, lamb, cow's milk, cat, and dog but not turkey, chicken, or fish. Absorption experiments indicated that this pattern of sensitivity was explained by an IgE antibody specific for alpha-gal.
We report a novel and severe food allergy related to IgE antibodies to the carbohydrate epitope alpha-gal. These patients experience delayed symptoms of anaphylaxis, angioedema, or urticaria associated with eating beef, pork, or lamb.

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Available from: Scott P Commins, Oct 07, 2015
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    • "In addition, lipid transfer protein found in fruits such as peach is a common trigger of food-induced anaphylaxis in southern Europe.19 Lastly, Commins et al20 identified 24 patients with a history of delayed onset of anaphylaxis or urticaria occurring 3–6 hours after the ingestion of meat, who have IgE antibodies to galactose-alpha-1,3-galactose (alpha-gal), a carbohydrate commonly expressed on non-primate mammalian proteins. The diagnosis of food allergy is based on clinical history, measurement of food-specific IgE in the serum, by skin-prick testing, and confirmatory oral food challenge. "
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    Journal of Asthma and Allergy 07/2014; 7(7):95-104. DOI:10.2147/JAA.S48611
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    • "Galactose-α-1,3-galactose (α-Gal) is a sugar structure found on glycoproteins and glycolipids of non-primate mammals and new world monkeys, but not on humans. IgE-antibodies specific for α-Gal (anti-α-Gal-IgE) may be associated with severe allergic symptoms and with delayed-type anaphylaxis [58,59]. α-Gal is also present on cat IgA which does not show high allergenic activity [60], and on gelatine containing material. "
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    • "Patients with pre-formed IgE antibodies to α-gal were found to suffer from anaphylactic reactions upon first exposure with cetuximab, a chimeric therapeutic antibody with murine variable domains that contains the α-gal epitope [5]. Moreover, cases of meat allergy have also been linked to IgE anti-α-gal [6]–[8]. "
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    ABSTRACT: IgE antibodies to gal-α-1,3-gal-β-1,4-GlcNAc (α-gal) can mediate a novel form of delayed anaphylaxis to red meat. Although IgG antibodies to α-gal (anti-α-gal or anti-Gal) are widely expressed in humans, IgE anti-α-gal is not. We explored the relationship between the IgG and IgE responses to both α-gal and the related blood group B antigen. Contradicting previous reports, antibodies to α-gal were found to be significantly less abundant in individuals with blood group B or AB. Importantly, we established a connection between IgE and IgG responses to α-gal: elevated titers of IgG anti-α-gal were found in IgE-positive subjects. In particular, proportionally more IgG1 anti-α-gal was found in IgE-positive subjects against a background of IgG2 production specific for α-gal. Thus, two types of immune response to α-gal epitopes can be distinguished: a 'typical' IgG2 response, presumably in response to gut bacteria, and an 'atypical', Th2-like response leading to IgG1 and IgE in addition to IgG2. These results suggest that IgE to a carbohydrate antigen can be formed (probably as part of a glycoprotein or glycolipid) even against a background of bacterial immune stimulation with essentially the same antigen.
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