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Tropomyosin Contains IgE-Binding Epitopes Sensitive to Periodate but Not to Enzymatic Deglycosylation

Authors

  • Wei-Wei Ruan,

    1. College of Biological Engineering, The Key Laboratory of Science and Technology for Aquaculture and Food Safety, Jimei Univ., Xiamen, Fujian 361021, China
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  • Min-Jie Cao,

    1. College of Biological Engineering, The Key Laboratory of Science and Technology for Aquaculture and Food Safety, Jimei Univ., Xiamen, Fujian 361021, China
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  • Feng Chen,

    1. Dept. of Food, Nutrition, and Packaging Sciences, Clemson Univ., Clemson, SC 29634, U.S.A.
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  • Qiu-Feng Cai,

    1. College of Biological Engineering, The Key Laboratory of Science and Technology for Aquaculture and Food Safety, Jimei Univ., Xiamen, Fujian 361021, China
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  • Wen-Jin Su,

    1. College of Biological Engineering, The Key Laboratory of Science and Technology for Aquaculture and Food Safety, Jimei Univ., Xiamen, Fujian 361021, China
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  • You-Zhao Wang,

    1. College of Biological Engineering, The Key Laboratory of Science and Technology for Aquaculture and Food Safety, Jimei Univ., Xiamen, Fujian 361021, China
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  • Guang-Ming Liu

    Corresponding author
    • College of Biological Engineering, The Key Laboratory of Science and Technology for Aquaculture and Food Safety, Jimei Univ., Xiamen, Fujian 361021, China
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Direct inquiries to author Liu (E-mail: gmliu@jmu.edu.cn).

Abstract

Glycosylation has been reported to affect the epitopes of food allergens, however, there are few reports on its role in crab allergen. In the present study, the effect of glycosylation on the IgE-binding activity of tropomyosin (TM), a major allergen in Scylla paramamosain, was investigated. The results showed that TM was a glycoprotein with a 0.2% carbohydrate moiety and contained O-glycan. Moreover, enzymatic deglycosylation of TM by glycosidase had no effect on the IgE-binding activity of TM. In contrast, treatment with periodate resulted in a significant reduction in its IgE-binding activity.

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