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A single amino acid substitution on the surface of a natural hevein isoform (Hev b 6.0202), confers different IgE recognition
Author(s) -
Reyes-López César A.,
Pedraza-Escalona Martha,
Mendoza Guillermo,
Hernández-Santoyo Alejandra,
Rodríguez-Romero Adela
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.03.085
Subject(s) - substitution (logic) , gene isoform , chemistry , amino acid substitution , immunoglobulin e , biochemistry , amino acid , biology , antibody , computer science , gene , immunology , mutation , programming language
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 (∼27%) with the isoallergen. Overall, these results are relevant to delineate crucial residues involved in this dominant discontinuous epitope.