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Structural bioinformatic approaches to understand cross‐reactivity
Author(s) -
Breiteneder Heimo,
Mills Clare
Publication year - 2006
Publication title -
molecular nutrition and food research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.495
H-Index - 131
eISSN - 1613-4133
pISSN - 1613-4125
DOI - 10.1002/mnfr.200500274
Subject(s) - cross reactivity , reactivity (psychology) , chemistry , immunoglobulin e , allergen , cross reactions , food allergens , computational biology , structural similarity , plant lipid transfer proteins , antibody , immunology , biochemistry , biology , allergy , medicine , alternative medicine , pathology , gene
Cross‐reactivity of allergens results from the presence of antibody‐accessible conserved surface structures. These can best be studied when allergens have been structurally defined by X‐ray crystallography or another structure determination method. When this is not the case, mimotope technology provides a useful alternative for elucidating antibody‐binding sites on allergens. Structural bioinformatic approaches have been used to study the cross‐reactivity of inhalant allergens with labile food allergens (Bet v 1 family) as well as the cross‐reactivity between stable food allergens such as members of the nonspecific lipid transfer protein family. It was found that the degree of similarity of the structures correlated with the observed IgE cross‐reactivities. However, IgE cross‐reactivity between structurally unrelated allergens has not been demonstrated to date.