A single amino acid substitution on the surface of a natural hevein isoform (Hev b 6.0202), confers different IgE recognition

FEBS Letters
César A Reyes-LópezAdela Rodríguez-Romero

Abstract

Decreased immune reactivity of isoforms of major allergens has been reported. However, such claims have always been based on experiments with recombinant proteins. This work describes the molecular and physicochemical characterization of a hevein (Hev b 6.0201) natural isoform (Hev b 6.0202), which is present in rubber latex from Hevea brasiliensis. The isoallergen has a single substitution Asn14Asp, which gives rise to local differences in the surface potential, as observed from the crystal structure presented here. Besides, ELISA inhibition using serum pools of adult and pediatric patients showed reduced IgE-binding capacity ( approximately 27%) with the isoallergen. Overall, these results are relevant to delineate crucial residues involved in this dominant discontinuous epitope.

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Citations

Aug 19, 2007·International Archives of Allergy and Immunology·Kyoung Yong JeongTai-Soon Yong
Jan 26, 2016·Biochimica Et Biophysica Acta·Karine BerthelotFrédéric Peruch
Oct 22, 2008·Molecular Immunology·Martha Pedraza-EscalonaAdela Rodríguez-Romero
Apr 14, 2011·Yonsei Medical Journal·Kyoung Yong JeongJung-Won Park
Jun 19, 2016·Biochimie·Karine BerthelotSophie Lecomte
Mar 11, 2018·Biochemistry. Biokhimii︠a︡·A A SlavokhotovaT I Odintsova

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