Abstract
The use of sweet lupins as a new food is resulting in an increasing number of cases of allergy reactions, particularly in atopic patients with other pre-existing legume allergies. We performed an extensive in silico analysis of seed β-conglutins, a new family of major allergen proteins in lupin, and a comparison to other relevant food allergens such as Ara h 1. We analyzed surface residues involved in conformational epitopes, lineal B- and T-cell epitopes variability, and changes in 2-D structural elements and 3D motives, with the aim to investigate IgE-mediated cross-reactivity among lupin, peanut, and other different legumes.
Our results revealed that considerable structural differences exist, parti- cularly affecting 2-D elements (loops and coils), and numerous micro-hetero-geneities are present in fundamental residues directly involved in epitopes variability.
Variability of residues involved in IgE-binding epitopes might be a major contributor to the observed differences in cross-reactivity among legumes.
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Jimenez-Lopez, J.C., Lima-Cabello, E., Melser, S., Foley, R.C., Singh, K.B., Juan D., A. (2015). Lupin Allergy: Uncovering Structural Features and Epitopes of β-conglutin Proteins in Lupinus Angustifolius L. with a Focus on Cross-allergenic Reactivity to Peanut and Other Legumes. In: Ortuño, F., Rojas, I. (eds) Bioinformatics and Biomedical Engineering. IWBBIO 2015. Lecture Notes in Computer Science(), vol 9043. Springer, Cham. https://doi.org/10.1007/978-3-319-16483-0_10
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DOI: https://doi.org/10.1007/978-3-319-16483-0_10
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