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.
Perspectives
We suggest that the structural study of endogenous allergens containing modifications such as glycosylations is relevant to investigate the immune responses against them by the host. These analyses should be considered in the future design of diagnostic tools and allergy therapies.
Rodriguez-Romero Adela
Universidad Nacional Autonoma de Mexico
Read the Original
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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