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We used Gad m 1 as the fish \u03b2-parvalbumin model and a combination of approaches, including peptide arrays, recombinant wt and mutant chains, biophysical characterizations, protease digestions, mass spectrometry, dot-blot and ELISA assays to gain insights into the role of amyloids in the IgE interaction. We found that Gad m 1 immunoreactive regions behave as sequence-dependent conformational epitopes that provide a 1000-fold increase in affinity and the structural repetitiveness required for optimal IgE binding and cross-linking upon folding into amyloids. These findings support the amyloid state as a key entity in type I food allergy.<\/jats:p>","DOI":"10.1038\/srep32801","type":"journal-article","created":{"date-parts":[[2016,9,6]],"date-time":"2016-09-06T09:36:27Z","timestamp":1473154587000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":27,"title":["The amyloid fold of Gad m 1 epitopes governs IgE binding"],"prefix":"10.1038","volume":"6","author":[{"given":"Rosa","family":"S\u00e1nchez","sequence":"first","affiliation":[]},{"given":"Javier","family":"Mart\u00ednez","sequence":"additional","affiliation":[]},{"given":"Ana","family":"Castro","sequence":"additional","affiliation":[]},{"given":"Mar\u00eda","family":"Pedrosa","sequence":"additional","affiliation":[]},{"given":"Santiago","family":"Quirce","sequence":"additional","affiliation":[]},{"given":"Rosa","family":"Rodr\u00edguez-P\u00e9rez","sequence":"additional","affiliation":[]},{"given":"Mar\u00eda","family":"Gasset","sequence":"additional","affiliation":[]}],"member":"297","published-online":{"date-parts":[[2016,9,6]]},"reference":[{"key":"BFsrep32801_CR1","doi-asserted-by":"publisher","first-page":"3487","DOI":"10.1073\/pnas.0915166107","volume":"107","author":"L Goldschmidt","year":"2010","unstructured":"Goldschmidt, L., Teng, P. 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