Please use this identifier to cite or link to this item: https://hdl.handle.net/20.500.12530/25337
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dc.contributor.authorSánchez, Rosa
dc.contributor.authorMartínez, Javier
dc.contributor.authorCastro, Ana
dc.contributor.authorPedrosa, María
dc.contributor.authorQuirce, Santiago
dc.contributor.authorRodríguez-Pérez, Rosa
dc.contributor.authorGasset, María
dc.date.accessioned2019-06-28T14:32:38Z-
dc.date.available2019-06-28T14:32:38Z-
dc.date.issued2016
dc.identifier.citationSci Rep.2016 09;(6):32801
dc.identifier.urihttps://hdl.handle.net/20.500.12530/25337-
dc.description.abstractAmyloids are polymeric structural states formed from locally or totally unfolded protein chains that permit surface reorganizations, stability enhancements and interaction properties that are absent in the precursor monomers. β-Parvalbumin, the major allergen in fish allergy, forms amyloids that are recognized by IgE in the patient sera, suggesting a yet unknown pathological role for these assemblies. We used Gad m 1 as the fish β-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.
dc.language.isoeng
dc.rightsopenAccess-
dc.subject.meshAllergens
dc.subject.meshAmino Acid Sequence
dc.subject.meshAmyloid
dc.subject.meshAmyloidogenic Proteins
dc.subject.meshAmyloidosis
dc.subject.meshAnimals
dc.subject.meshChild
dc.subject.meshEpitopes
dc.subject.meshFemale
dc.subject.meshFishes
dc.subject.meshFood Hypersensitivity
dc.subject.meshHumans
dc.subject.meshImmunoglobulin E
dc.subject.meshMale
dc.subject.meshParvalbumins
dc.subject.meshProtein Binding
dc.titleThe amyloid fold of Gad m 1 epitopes governs IgE binding.
dc.typeArtículo
dc.identifier.pubmedID27597317
dc.format.volume6
dc.format.page32801
dc.identifier.e-issn2045-2322
dc.identifier.journalScientific reports
dc.identifier.doi10.1038/srep32801
dc.identifier.pmcPMC5011719
dc.pubmedtypeJournal Article
dc.pubmedtypeResearch Support, Non-U.S. Gov't
Appears in Collections:Fundaciones e Institutos de Investigación > IIS H. U. La Paz > Artículos
Hospitales > H. U. La Paz > Artículos

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