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- W2044895514 abstract "Post translational modifications of a seed storage protein, barley γ3-hordein, were determined using immunochemical and mass spectrometry methods. IgE reactivity towards this protein was measured using sera from patients diagnosed with allergies to wheat. N-glycosylation was found at an atypical Asn-Leu-Cys site. The observed glycan contains xylose. This indicates that at least some γ3-hordein molecules trafficked through the Golgi apparatus. Disulfide bridges in native γ3-hordein were almost the same as those found in wheat γ46-gliadin, except the bridge involving the cysteine included in the glycosylation site. IgE reacted more strongly towards the recombinant than the natural γ3-hordein protein. IgE binding to γ3-hordein increased when the protein sample was reduced. Glycosylation and disulfide bridges therefore decrease epitope accessibility. Thus the IgE from patients sensitized to wheat cross-react with γ3-hordein due to sequence homology with wheat allergens rather than through shared carbohydrate determinants." @default.
- W2044895514 created "2016-06-24" @default.
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- W2044895514 date "2013-01-01" @default.
- W2044895514 modified "2023-10-15" @default.
- W2044895514 title "Barley γ3-hordein: Glycosylation at an atypical site, disulfide bridge analysis, and reactivity with IgE from patients allergic to wheat" @default.
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- W2044895514 doi "https://doi.org/10.1016/j.bbapap.2012.07.016" @default.
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