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Identification of IgE-binding peptide and critical amino acids of Jatropha curcas allergen involved in allergenic response
Increasing energy demand has spurred interest in the use of biofuels. Jatropha curcas (physic nut), an inedible oilseed, is a potential source of bioenergy. The seeds, however, contain allergens such as Jat c 1, a 2S albumin that can induce hypersensitivity reactions in humans and result in allergic...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer International Publishing
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4831952/ https://www.ncbi.nlm.nih.gov/pubmed/27119058 http://dx.doi.org/10.1186/s40064-016-2036-5 |
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author | Crespo, Livia Maia de Oliveira, Natalia Deus Damatta, Renato Augusto do Nascimento, Viviane Veiga Soares, Thais Pacheco Machado, Olga Lima Tavares |
author_facet | Crespo, Livia Maia de Oliveira, Natalia Deus Damatta, Renato Augusto do Nascimento, Viviane Veiga Soares, Thais Pacheco Machado, Olga Lima Tavares |
author_sort | Crespo, Livia Maia |
collection | PubMed |
description | Increasing energy demand has spurred interest in the use of biofuels. Jatropha curcas (physic nut), an inedible oilseed, is a potential source of bioenergy. The seeds, however, contain allergens such as Jat c 1, a 2S albumin that can induce hypersensitivity reactions in humans and result in allergic diseases. Recent advances in identifying and characterizing plant allergens and, in particular, their immunoglobulin E (IgE)-binding epitopes have produced a wealth of information. We identified IgE-binding regions and the critical amino acids involved in the degranulation of mast cells and the release of histamine, preliminary steps for the prevention and treatment of this allergy. Four IgE-binding regions were identified in the sequence of Jat c 1. We identified and demonstrated the fundamental role of two glutamic acid residues in IgE binding. The sequence LEKQLEEGEVGS produces a random loop on the most exposed part of Jat c 1. This region is important to the stimulation of the allergic response. The possibility of using this information to produce vaccines and other pharmacological agents for allergy treatment is discussed. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s40064-016-2036-5) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-4831952 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Springer International Publishing |
record_format | MEDLINE/PubMed |
spelling | pubmed-48319522016-04-26 Identification of IgE-binding peptide and critical amino acids of Jatropha curcas allergen involved in allergenic response Crespo, Livia Maia de Oliveira, Natalia Deus Damatta, Renato Augusto do Nascimento, Viviane Veiga Soares, Thais Pacheco Machado, Olga Lima Tavares Springerplus Research Increasing energy demand has spurred interest in the use of biofuels. Jatropha curcas (physic nut), an inedible oilseed, is a potential source of bioenergy. The seeds, however, contain allergens such as Jat c 1, a 2S albumin that can induce hypersensitivity reactions in humans and result in allergic diseases. Recent advances in identifying and characterizing plant allergens and, in particular, their immunoglobulin E (IgE)-binding epitopes have produced a wealth of information. We identified IgE-binding regions and the critical amino acids involved in the degranulation of mast cells and the release of histamine, preliminary steps for the prevention and treatment of this allergy. Four IgE-binding regions were identified in the sequence of Jat c 1. We identified and demonstrated the fundamental role of two glutamic acid residues in IgE binding. The sequence LEKQLEEGEVGS produces a random loop on the most exposed part of Jat c 1. This region is important to the stimulation of the allergic response. The possibility of using this information to produce vaccines and other pharmacological agents for allergy treatment is discussed. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s40064-016-2036-5) contains supplementary material, which is available to authorized users. Springer International Publishing 2016-04-14 /pmc/articles/PMC4831952/ /pubmed/27119058 http://dx.doi.org/10.1186/s40064-016-2036-5 Text en © Crespo et al. 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Research Crespo, Livia Maia de Oliveira, Natalia Deus Damatta, Renato Augusto do Nascimento, Viviane Veiga Soares, Thais Pacheco Machado, Olga Lima Tavares Identification of IgE-binding peptide and critical amino acids of Jatropha curcas allergen involved in allergenic response |
title | Identification of IgE-binding peptide and critical amino acids of Jatropha curcas allergen involved in allergenic response |
title_full | Identification of IgE-binding peptide and critical amino acids of Jatropha curcas allergen involved in allergenic response |
title_fullStr | Identification of IgE-binding peptide and critical amino acids of Jatropha curcas allergen involved in allergenic response |
title_full_unstemmed | Identification of IgE-binding peptide and critical amino acids of Jatropha curcas allergen involved in allergenic response |
title_short | Identification of IgE-binding peptide and critical amino acids of Jatropha curcas allergen involved in allergenic response |
title_sort | identification of ige-binding peptide and critical amino acids of jatropha curcas allergen involved in allergenic response |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4831952/ https://www.ncbi.nlm.nih.gov/pubmed/27119058 http://dx.doi.org/10.1186/s40064-016-2036-5 |
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