Structural insights into the IgE mediated responses induced by the allergens Hev b 8 and Zea m 12 in their dimeric forms

dc.contributorNature Publishing Group
dc.creatorMares Mejía, Israel
dc.creatorMartínez Caballero, Siseth
dc.creatorGaray Canales, Claudia
dc.creatorCano Sánchez, Patricia
dc.creatorTorres Larios, Alfredo
dc.creatorLara González, Samuel
dc.creatorOrtega, Enrique
dc.creatorRodriguez Romero, Adela
dc.date2018-03-23T23:59:53Z
dc.date2018-03-23T23:59:53Z
dc.date2016-09
dc.date.accessioned2023-07-17T22:03:14Z
dc.date.available2023-07-17T22:03:14Z
dc.identifierMares-Mejía, I. et al. Structural insights into the IgE mediated responses induced by the allergens Hev b 8 and Zea m 12 in their dimeric forms. Sci. Rep. 6, 32552; doi: 10.1038/srep32552 (2016).
dc.identifierhttp://hdl.handle.net/11627/3735
dc.identifierhttps://doi.org/10.1038/srep32552
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/7543410
dc.description"Oligomerization of allergens plays an important role in IgE-mediated reactions, as effective crosslinking of IgE-Fc epsilon RI complexes on the cell membrane is dependent on the number of exposed B-cell epitopes in a single allergen molecule or on the occurrence of identical epitopes in a symmetrical arrangement. Few studies have attempted to experimentally demonstrate the connection between allergen dimerization and the ability to trigger allergic reactions. Here we studied plant allergenic profilins rHev b 8 (rubber tree) and rZea m 12 (maize) because they represent an important example of cross-reactivity in the latex-pollen-food syndrome. Both allergens in their monomeric and dimeric states were isolated and characterized by exclusion chromatography and mass spectrometry and were used in immunological in vitro experiments. Their crystal structures were solved, and for Hev b 8 a disulfide-linked homodimer was found. Comparing the structures we established that the longest loop is relevant for recognition by IgE antibodies, whereas the conserved regions are important for cross-reactivity. We produced a novel monoclonal murine IgE (mAb 2F5), specific for rHev b 8, which was useful to provide evidence that profilin dimerization considerably increases the IgE-mediated degranulation in rat basophilic leukemia cells."
dc.formatapplication/pdf
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.rightsAcceso Abierto
dc.subjectImmunology
dc.subjectX-ray crystallography
dc.subjectCIENCIAS TECNOLÓGICAS
dc.titleStructural insights into the IgE mediated responses induced by the allergens Hev b 8 and Zea m 12 in their dimeric forms
dc.typearticle


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