Review: Mapping of IgE-binding epitopes on the major latex allergen Hev b 2 and the cross-reacting 1,3 beta -glucanase fruit allergens as a molecular basis for the latex-fruit syndrome

• Published in: Molecular immunology 2009-05, Vol.46 (8-9), p.1595-1604
• Main Authors: Barre, Annick, Culerrier, Raphael, Granier, Claude, Selman, Laetitia, Peumans, Willy J, Van Damme, Els J M, Bienvenu, Francoise, Bienvenu, Jacques, Rouge, Pierre
• Format: Article
• Language: English
• Subjects: Hepatitis E virus; Musa; Olea
• ISSN: 0161-5890
• DOI: 10.1016/j.molimm.2008.12.007

Nine distinct IgE-binding epitopes were identified along the entire amino acid sequence of the major latex allergen Hev b 2 (1,3 beta -glucanase) using a set of synthetic 15-mer peptides frameshifted by 3 residues immobilized on cellulose membrane (Spot technique). Most of the amino acid residues building these IgE-binding epitopic regions are nicely exposed on the surface and the epitopes usually correspond to charged regions on the molecular surface of the protein. A smaller number of 5 IgE-binding epitopic areas was identified on the banana 1,3 beta -glucanase, which exhibits a very similar overall conformation and charge distribution. The latter epitopes might be responsible for the IgE-binding cross-reactivity currently observed in the latex-fruit syndrome. Using rabbit polyclonal IgG anti-BanGluc as a probe instead of IgE from allergic patients the same epitopic regions were identified in both Hev b 2 and BanGluc. Additionally, surface-exposed regions with a very close conformation were predicted to occur on Ole e 9, the 1,3 beta -glucanase allergen identified in olive pollen.