Laminin γ-1 and collagen α-1 (VI) chain are galactose-α-1,3-galactose-bound allergens in beef

Takahashi, Hitoshi; Chinuki, Yuko; Tanaka, Ayaki; Morita, Eishin

doi:10.1111/all.12302

Cited by 57 publications

(44 citation statements)

References 29 publications

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“…Recently, it has been reported that laminin c-1 and collagen a-1 (VI) chain from beef are a-Gal-containing allergens (21). Those findings were in line with previous research demonstrating cross-reactivity of red meat with gelatin, a derivative of collagen (7), and that laminins contain a-Gal at the post-translational modification level (22).…”

supporting

confidence: 89%

Immunoproteomics of processed beef proteins reveal novel galactose‐α‐1,3‐galactose‐containing allergens

Apostolović

Tran

Hamsten

et al. 2014

Allergy

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supporting

confidence: 89%

Immunoproteomics of processed beef proteins reveal novel galactose‐α‐1,3‐galactose‐containing allergens

Apostolović

Tran

Hamsten

et al. 2014

Allergy

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“…Proteomics is an important tool in revealing and assessing the physicochemical properties of food allergens 16, 17 and several proteomics studies have identified α-Gal-containing meat proteins that react with IgE from red meat-allergic patients 18–20 . Some of these proteins remain stable to thermal processing, showing that the allergenic properties are preserved in cooked meat 19, 20 .…”

Section: Introductionmentioning

confidence: 99%

Peptidomics of an in vitro digested α-Gal carrying protein revealed IgE-reactive peptides

Apostolović

Krstic

Mihailović

et al. 2017

Sci Rep

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The mammalian carbohydrate galactose-α1,3-galactose (α-Gal) causes a novel form of food allergy, red meat allergy, where patients experience severe allergic reactions several hours after red meat consumption. Here we explored gastric digestion of α-Gal glycoproteins using an in vitro model. Bovine thyroglobulin (BTG), a typical α-Gal carrying glycoprotein, was digested with pepsin. The resulting peptides were characterised by SDS PAGE, immunoblot and ImmunoCAP using sera from 20 red meat allergic patients. During pepsinolysis of BTG, a wide range of peptide bands was observed of which 14 to 17 kDa peptides remained stable throughout the gastric phase. The presence of the α-Gal epitope on the obtained peptides was demonstrated by an anti-α-Gal antibody and IgE from red meat allergic patients. The α-Gal digests were able to inhibit up to 86% of IgE reactivity to BTG. Importantly, basophil activation test demonstrated that the allergenic activity of BTG was retained after digestion in all four tested patients. Mass spectrometry-based peptidomics revealed that these peptides represent mostly internal and C-terminal parts of the protein, where the most potent IgE-binding α-Gal residues were identified at Asn1756, Asn1850 and Asn2231. Thus allergenic α-Gal epitopes are stable to pepsinolysis, reinforcing their role as clinically relevant food allergens.

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“…20 Briefly, proteins were separated using SDS-polyacrylamide gel electrophoresis (SDS-PAGE). Serum shrimp-specific IgE, crab-specific IgE, squid-specific IgE, tropomyosin-specific IgE, Der p 1 (peptidase 1)-specific IgE, and Der p 10 (tropomyosin)-specific IgE levels were detected by the CAP-fluorescent-enzyme immunoassays (CAP-FEIA) (ImmunoCAP â , ThermoFischer Scientific, Uppsala, Sweden).…”

Section: Measurement Of Serum Allergen-specific Igementioning

confidence: 99%

“…20 Briefly, water-soluble and water-insoluble shrimp proteins were separated on 12.5% SDS-PAGE under reducing condition and electrophoretically transferred to a PVDF membrane. 20 Briefly, water-soluble and water-insoluble shrimp proteins were separated on 12.5% SDS-PAGE under reducing condition and electrophoretically transferred to a PVDF membrane.…”

Section: Sodium Periodate Treatmentmentioning

confidence: 99%

Tropomyosin is a minor but distinct allergen in patients with shrimp allergies in Japan

Tsedendorj

Chinuki

Ueda

et al. 2018

J Cutaneous Imm & Allergy

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Recently, purified allergens have been utilized for allergen-specific IgE tests, which are highly useful because of their excellent specificity and sensitivity in identifying allergic patients. The purpose of this study was to evaluate the specificity and sensitivity of tropomyosin-specific IgE test in the diagnosis of shrimp allergies in Japan.We enrolled 27 patients with shrimp allergy and five patients with atopic dermatitis, who had no history of allergic reactions to shrimp but showed positive results in tropomyosin-specific IgE test, in this study. Tropomyosin-specific IgE was determined by IgE immunoblotting and tropomyosin-specific IgE test. Involvement of carbohydrate moieties in IgE binding to the allergens was examined by periodate treatment. Tropomyosin-specific IgE was detected in 13 and positive in 10 of the 27 patients with shrimp allergy, whereas shrimp-specific IgE was detected in 21 and positive in 20 of these 27 patients. Of the 13 patients with detectable levels of tropomyosin-specific IgE, seven were confirmed to have tropomyosin-specific IgE by immunoblotting analysis, whereas no IgE binding was seen in the five patients with atopic dermatitis, indicating the high specificity of the tropomyosin-specific IgE test.The level of tropomyosin-specific IgE was well correlated with those of shrimp-specific IgE and Der p 10-specific IgE. Our findings indicated tropomyosin is a minor but distinct allergen in patients with shrimp allergy, especially causing symptoms of OAS. K E Y W O R D Scross-reactivity, crustaceans, shellfish, shrimp, tropomyosin

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Laminin γ-1 and collagen α-1 (VI) chain are galactose-α-1,3-galactose-bound allergens in beef

Abstract: The carbohydrate moiety (α-Gal) on laminin γ-1 and collagen α-1 (VI) chain are possibly common IgE-reactive proteins in the Japanese patients with beef allergy.

Cited by 57 publications

References 29 publications

Immunoproteomics of processed beef proteins reveal novel galactose‐α‐1,3‐galactose‐containing allergens

Immunoproteomics of processed beef proteins reveal novel galactose‐α‐1,3‐galactose‐containing allergens

Peptidomics of an in vitro digested α-Gal carrying protein revealed IgE-reactive peptides

Tropomyosin is a minor but distinct allergen in patients with shrimp allergies in Japan

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