Utilize este identificador para referenciar este registo: http://hdl.handle.net/10400.18/2433
Título: Maize IgE binding proteins: each plant a different profile?
Autor: Fonseca, Cátia
Planchon, Sébastien
Pinheiro, Carla
Renaut, Jenny
Ricardo, Cândido
Oliveira, M. Margarida
Batista, Rita
Palavras-chave: Segurança Alimentar
Maize Allergens
Western-blot
2D-gel Electrophoresis
Maize Proteins
Data: 20-Mar-2014
Editora: BioMed Central
Citação: Proteome Sci. 2014 Mar 20;12(1):17. doi: 10.1186/1477-5956-12-17
Resumo: Background: Allergies are nearly always triggered by protein molecules and the majority of individuals with documented immunologic reactions to foods exhibit IgE hypersensitivity reactions. In this study we aimed to understand if natural differences, at proteomic level, between maize populations, may induce different IgE binding proteins profiles among maize-allergic individuals. We also intended to deepen our knowledge on maize IgE binding proteins. Results: In order to accomplish this goal we have used proteomic tools (SDS-PAGE and 2-D gel electrophoresis followed by western blot) and tested plasma IgE reactivity from four maize-allergic individuals against four different protein fractions (albumins, globulins, glutelins and prolamins) of three different maize cultivars. We have observed that maize cultivars have different proteomes that result in different IgE binding proteins profiles when tested against plasma from maize-allergic individuals. We could identify 19 different maize IgE binding proteins, 11 of which were unknown to date. Moreover, we found that most (89.5%) of the 19 identified potential maize allergens could be related to plant stress. Conclusions: These results lead us to conclude that, within each species, plant allergenic potential varies with genotype. Moreover, considering the stress-related IgE binding proteins identified, we hypothesise that the environment, particularly stress conditions, may alter IgE binding protein profiles of plant components.
Peer review: yes
URI: http://hdl.handle.net/10400.18/2433
DOI: doi: 10.1186/1477-5956-12-17
ISSN: 1477-5956
Versão do Editor: http://www.proteomesci.com/content/12/1/17
Aparece nas colecções:DAN - Artigos em revistas internacionais

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