Abstract - IgE Antibody Binding to the Carbohydrate Moiety of Hev b 13


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	Publications of MRB Latest Publications MRB Digest Journal of Rubber Research 3^rd Qtr 2008 Vol 11(3) 2^nd Qtr 2008 Vol 11(2) 1^st Qtr 2008 Vol 11(1) 4^th Qtr 2007 Vol 10(4) 3^rd Qtr 2007 Vol 10(3) 2^nd Qtr 2007 Vol 10(2) 1^st Qtr 2007 Vol 10(1) 1^st Qtr 2006 Vol 9(1) 2^nd Qtr 2006 Vol 9(2) 3^rd Qtr 2006 Vol 9(3) 4^th Qtr 2006 Vol 9(4) Submit paper/article Order Form	Abstract IgE Antibody Binding to the Carbohydrate Moiety of Hev b 13 S.A.M Arif, RG Hamilton and HY Yeang 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 is due 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. back
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