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The red meat allergy syndrome in Sweden

View Article: PubMed Central - PubMed

ABSTRACT

In the last decade, a novel type of food allergy presenting with severe allergic reactions several hours after consumption of red meat has been recognized. The allergic responses are due to IgE antibodies directed against the carbohydrate epitope galactose-α-1,3-galactose (α-Gal) found in mammalian meat. This review presents the red meat allergy syndrome in Sweden, discusses the features of the immune response to carbohydrates, and highlights the presence of heat stable α-Gal-containing proteins in meat.

The number of diagnosed red meat allergy cases in Sweden has increased significantly over the past few years. All patients have been tick bitten. Our recent work has shown that α-Gal is present in the European tick Ixodes ricinus (I. ricinus), thus potentially explaining the strong association between anti-α-Gal IgE and tick bites, with development of red meat allergy as a secondary phenomenon. Further studies using immunoproteomics have identified novel α-Gal-containing meat proteins that bound IgE from red meat allergic patients. Four of these proteins were stable to thermal processing pointing to the fact that the allergenicity of red meat proteins is preserved in cooked meat. In keeping with the fact that the α-Gal epitope is structurally related to the blood group B antigen, a positive association with the B-negative blood groups among our red meat allergic patients was noted. A selective IgE reactivity to the pure carbohydrate moiety was observed when investigating the specificity of the α-Gal immune response. IgE from red meat allergic patients does not recognize the other major mammalian carbohydrate, N-glycolylneuraminic acid (Neu5Gc), also present in high amounts in red meat. Furthermore, neither common cross-reactive carbohydrate determinants (CCDs) from plants nor venoms are targets of the IgE response in these patients.

Taken together, the α-Gal carbohydrate has shown to be a potentially clinically relevant allergen that should be taken into account in the diagnosis of food allergy. Many new findings in the field of red meat allergy have been obtained during the past years, but further efforts to understand the process of digestion, absorption, and delivery of α-Gal-containing molecules to the circulation are needed.

No MeSH data available.


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Mentions: We characterized the proteomic profile of different beef preparations (raw, medium rare, fried, and boiled) and investigated their potential allergenicity among Swedish red meat allergic patients. We noted that most of the red meat allergic patients recognized similar IgE-binding proteins of beef in a wide range of molecular weight (25–250 kDa) [30]. The IgE reactivity was stronger to raw and medium rare meat compared to fried and boiled meat. Using an immunoproteomic approach, we identified 18 proteins from Bos taurus, seven of them contained α-Gal (Fig.1). When examining different processed beef preparations, four IgE-binding α-Gal-containing proteins were shown to be stable to heat treatment (creatine kinase M-type, aspartate aminotransferase, β-enolase, and α-enolase) [30]. These are cytoplasmic proteins, playing essential roles in the metabolic pathways [31, 32]. Thus, the allergenicity of red meat proteins carrying the α-Gal epitope is preserved even upon thermal processing. These findings indicate that even thermal cooking of red meat may induce a severe delayed allergic reaction. Moreover, we noticed that red meat allergic patients also have IgE responses to non-α-Gal-containing beef proteins.


The red meat allergy syndrome in Sweden
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC5016537&req=5

Mentions: We characterized the proteomic profile of different beef preparations (raw, medium rare, fried, and boiled) and investigated their potential allergenicity among Swedish red meat allergic patients. We noted that most of the red meat allergic patients recognized similar IgE-binding proteins of beef in a wide range of molecular weight (25–250 kDa) [30]. The IgE reactivity was stronger to raw and medium rare meat compared to fried and boiled meat. Using an immunoproteomic approach, we identified 18 proteins from Bos taurus, seven of them contained α-Gal (Fig.1). When examining different processed beef preparations, four IgE-binding α-Gal-containing proteins were shown to be stable to heat treatment (creatine kinase M-type, aspartate aminotransferase, β-enolase, and α-enolase) [30]. These are cytoplasmic proteins, playing essential roles in the metabolic pathways [31, 32]. Thus, the allergenicity of red meat proteins carrying the α-Gal epitope is preserved even upon thermal processing. These findings indicate that even thermal cooking of red meat may induce a severe delayed allergic reaction. Moreover, we noticed that red meat allergic patients also have IgE responses to non-α-Gal-containing beef proteins.

View Article: PubMed Central - PubMed

ABSTRACT

In the last decade, a novel type of food allergy presenting with severe allergic reactions several hours after consumption of red meat has been recognized. The allergic responses are due to IgE antibodies directed against the carbohydrate epitope galactose-α-1,3-galactose (α-Gal) found in mammalian meat. This review presents the red meat allergy syndrome in Sweden, discusses the features of the immune response to carbohydrates, and highlights the presence of heat stable α-Gal-containing proteins in meat.

The number of diagnosed red meat allergy cases in Sweden has increased significantly over the past few years. All patients have been tick bitten. Our recent work has shown that α-Gal is present in the European tick Ixodes ricinus (I. ricinus), thus potentially explaining the strong association between anti-α-Gal IgE and tick bites, with development of red meat allergy as a secondary phenomenon. Further studies using immunoproteomics have identified novel α-Gal-containing meat proteins that bound IgE from red meat allergic patients. Four of these proteins were stable to thermal processing pointing to the fact that the allergenicity of red meat proteins is preserved in cooked meat. In keeping with the fact that the α-Gal epitope is structurally related to the blood group B antigen, a positive association with the B-negative blood groups among our red meat allergic patients was noted. A selective IgE reactivity to the pure carbohydrate moiety was observed when investigating the specificity of the α-Gal immune response. IgE from red meat allergic patients does not recognize the other major mammalian carbohydrate, N-glycolylneuraminic acid (Neu5Gc), also present in high amounts in red meat. Furthermore, neither common cross-reactive carbohydrate determinants (CCDs) from plants nor venoms are targets of the IgE response in these patients.

Taken together, the α-Gal carbohydrate has shown to be a potentially clinically relevant allergen that should be taken into account in the diagnosis of food allergy. Many new findings in the field of red meat allergy have been obtained during the past years, but further efforts to understand the process of digestion, absorption, and delivery of α-Gal-containing molecules to the circulation are needed.

No MeSH data available.