Nine distinct IgE-binding epitopes were identified along the entire amino acid sequence of the major latex allergen Hev b 2 (1,3beta-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 1,3beta-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 1,3beta-glucanase allergen identified in olive pollen.