IgE antibody binding to the carbohydrate moiety of Hev b 13.

Siti Arija M. A., . IgE antibody binding to the carbohydrate moiety of Hev b 13. pp. 40-49. ISSN 1511-1768

Previous work has indicated the involvement of Hev b 13 glycan in the binding of specific human IgE antibodies. Further evidence is presented here to show that IgE binding to Hev b 13 isdue to its epitope(s) that reside(s) on the glycans covalently bound to the amino acid structure of the glycoprotein. Oxidative degradation of native Hev b 13 carbohydrate structures by periodate disabled most of the IgE antibody reactivity. To further study the role of the Hev b 13 glycan in IgE antibody-recognition an unglycosylated recombinant version of the protein was synthesised in Escherichia coli using the pMal-c2 vector. An 88 kDa protein was obtained which corresponded to the expected size of the MBP-Hev b 13 fusion protein. The recombinant protein was recognised by the monoclonal and polyclonal antibodies specific for Hev b 13 thus confirming its identity. However human IgE antibody failed to react with the unglycosylated recombinant Hev b 13 protein. Competitive inhibition of IgE binding to Hev b 13 by patatin was shown to result from cross-reacting carbohydrate determinants. These results indicated that the carbohydrate moiety of the glycoprotein played a principal role in human IgE antibody reactivity and allergenicity to Hev b 13.

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Abstract

Previous work has indicated the involvement of Hev b 13 glycan in the binding of specific human IgE antibodies. Further evidence is presented here to show that IgE binding to Hev b 13 isdue to its epitope(s) that reside(s) on the glycans covalently bound to the amino acid structure of the glycoprotein. Oxidative degradation of native Hev b 13 carbohydrate structures by periodate disabled most of the IgE antibody reactivity. To further study the role of the Hev b 13 glycan in IgE antibody-recognition an unglycosylated recombinant version of the protein was synthesised in Escherichia coli using the pMal-c2 vector. An 88 kDa protein was obtained which corresponded to the expected size of the MBP-Hev b 13 fusion protein. The recombinant protein was recognised by the monoclonal and polyclonal antibodies specific for Hev b 13 thus confirming its identity. However human IgE antibody failed to react with the unglycosylated recombinant Hev b 13 protein. Competitive inhibition of IgE binding to Hev b 13 by patatin was shown to result from cross-reacting carbohydrate determinants. These results indicated that the carbohydrate moiety of the glycoprotein played a principal role in human IgE antibody reactivity and allergenicity to Hev b 13.

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Item Type:	Article
AGROVOC Term:	Carbohydrates
AGROVOC Term:	Glycoproteins
AGROVOC Term:	Proteins
AGROVOC Term:	Allergens
AGROVOC Term:	Natural rubber
AGROVOC Term:	Biochemical oxidation
AGROVOC Term:	Antibodies
Geographical Term:	Malaysia
Depositing User:	Ms. Suzila Mohamad Kasim
Last Modified:	28 Apr 2025 03:11
URI:	http://webagris.upm.edu.my/id/eprint/22920

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