What is it about?
We describe the crystal structure of a natural allergen Hev b 2, (Beta-1,3-glucanase) that exhibits two glycosylation sites on its surface. These glycan moieties are asparagine-linked branched oligosaccharides with an alpha-1,3-fucosylation that has been associated with the allergenicity of plant and insect glycoproteins. Basophil cells stimulated with glycosylated Hev b 2 revealed greater cell activation and degranulation than the enzymatically deglycosylated allergen
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Why is it important?
These carbohydrate moieties on the surface of Hev b 2 constitute an important epitope that might be responsible for the IgE cross-reactivity that is observed in the latex-fruit syndrome.
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This page is a summary of: Structural analysis of the endogenous glycoallergen Hev b 2 (endo-β-1,3-glucanase) fromHevea brasiliensisand its recognition by human basophils, Acta Crystallographica Section D Biological Crystallography, January 2014, International Union of Crystallography,
DOI: 10.1107/s1399004713027673.
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