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Peptidomics of an i...
Peptidomics of an in vitro digested α-Gal carrying protein revealed IgE-reactive peptides
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- Apostolovic, D (författare)
- Karolinska Institutet
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Krstic, M (författare)
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Mihailovic, J (författare)
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Starkhammar, M (författare)
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Velickovic, TC (författare)
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- Hamsten, C (författare)
- Karolinska Institutet
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- van Hage, M (författare)
- Karolinska Institutet
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(creator_code:org_t)
- 2017-07-12
- 2017
- Engelska.
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Ingår i: Scientific reports. - : Springer Science and Business Media LLC. - 2045-2322. ; 7:1, s. 5201-
- Relaterad länk:
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https://doi.org/10.1...
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http://kipublication...
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https://doi.org/10.1...
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Abstract
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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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