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Mol Immunol ; 47(4): 871-7, 2010 Jan.
Article de Anglais | MEDLINE | ID: mdl-19945164

RÉSUMÉ

The three-dimensional model built for the major latex allergen Hev b 13 consists of the typical organization of plant esterases made of a central bundle of five parallel beta-strands surrounded by five alpha-helices associated to two shorter alpha-helical segments. Up to 12 sets of sequential IgE-binding peptides were identified in SPOT experiments along the amino acid sequence of Hev b 13. They correspond in fact to eight IgE-binding epitopic stretches exposed on the surface of the allergen. With the exception of epitope #5, all other epitopes contain charged residues. Epitope #8 contains the 3rd putative N-glycosylation site of Hev b 13 and should consist of a glycotope, whereas all other identified IgE-binding areas occur outside the two remaining putative N-glycosylation sites. Accordingly, the allergenicity of Hev b 13 does not primarily depends on its carbohydrate moiety.


Sujet(s)
Allergènes/composition chimique , Allergènes/immunologie , Glucides/immunologie , Esterases/immunologie , Hypersensibilité/immunologie , Latex/immunologie , Protéines végétales/composition chimique , Protéines végétales/immunologie , Caoutchouc/composition chimique , Adolescent , Adulte , Séquence d'acides aminés , Animaux , Antigènes végétaux , Bovins , Enfant , Cartographie épitopique , Femelle , Humains , Immunoglobuline E/immunologie , Mâle , Adulte d'âge moyen , Modèles moléculaires , Données de séquences moléculaires , Structure secondaire des protéines , Similitude de séquences d'acides aminés , Jeune adulte
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